Cited by 177Bacterial Genetics and BiotechnologyDrug Transport and Resistance MechanismsHeat shock proteins research

The DOI matches its Crossref record; 402 of the 402 references it cites were found in a registry or an index.

Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways.

Open access

Kudva, Renuka, Denks, Kärt, Kuhn, Patrick, Vogt, Andreas, Müller, Matthias, Koch, Hans-Georg·2013·Research in Microbiology

DOI 10.1016/j.resmic.2013.03.016

Open this paper in CoChat — free account Open PDF

Abstract

Gram negative bacteria possess a large variety of protein transport systems, by which proteins that are synthesised in the cytosol are exported to destinations in the cell envelope or entirely secreted into the extracellular environment. The inner membrane (IM) contains three major transport systems for the translocation and insertion of signal sequence containing proteins: the Sec translocon, the YidC insertase, and the Tat system. The heterotrimeric SecYEG translocon forms a narrow channel in the membrane that serves a dual function; it allows the translocation of unfolded proteins across the pore and the integration of α-helical proteins into the IM. The YidC insertase is a multi-spanning membrane protein that cooperates with the SecYEG translocon during the integration of membrane proteins but also functions as an independent insertase. Depending upon the type of protein cargo that needs to be transported, the Signal Recognition Particle (SRP), the SRP receptor, SecA and chaperones are required to coordinate translation with transport and to target and energise the different transport systems. The Tat system consists of three membrane proteins (TatA, TatB and TatC) which in a still unknown manner accomplish the transmembrane passage of completely folded proteins and protein complexes.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.resmic.2013.03.016

Cites

402 of 402 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Items 201–400 of 402

Distinct Requirements for Translocation of the N-tail and C-tail of the Escherichia coli Inner Membrane Protein CyoA
van Bloois, E., Haan, G.-J., Gier, J. D., Oudega, B., & Luirink, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511357200 · Cited by 81
Domain Interactions in E. coli SRP: Stabilization of M Domain by RNA Is Required for Effective Signal Sequence Modulation of NG Domain
Zheng, N., & Gierasch, L. M. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80009-x · Cited by 80
Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy
Walther, T. H., Grage, S. L., Roth, N., et al. (2010) · Journal of the American Chemical Society · doi:10.1021/ja106963s · Cited by 80
The Thylakoid Proton Gradient Promotes an Advanced Stage of Signal Peptide Binding Deep within the Tat Pathway Receptor Complex
rard, F. G., & Cline, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610337200 · Cited by 79
The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain
Moser, C., Mol, O., Goody, R. S., & Sinning, I. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11339 · Cited by 79
Disorder-order folding transitions underlie catalysis in the helicase motor of SecA
Keramisanou, D., Biris, N., Gelis, I., Sianidis, G., Spyridoula Karamanou, A., Economou, A., & Kalodimos, C. G. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1108 · Cited by 78
Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP
Junutula, J. R., Rodnina, M. V., & Wintermeyer, W. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3427 · Cited by 77
Structural basis of signal-sequence recognition by the signal recognition particle
Hainzl, T., Huang, S., Meriläinen, G., Brännström, K., & Sauer-Eriksson, A. E. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1994 · Cited by 77
The Escherichia coli twin‐arginine translocase: conserved residues of TatA and TatB family components involved in protein transport
Hicks, M. G., de Leeuw, E., Porcelli, I., et al. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00198-4 · Cited by 77
Evidence for a dynamic and transient pathway through the TAT protein transport machinery
Cline, K., & McCaffery, M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601759 · Cited by 77
Concentrations of 4.5S RNA and Ffh protein in Escherichia coli: the stability of Ffh protein is dependent on the concentration of 4.5S RNA
Jensen, C., & Pedersen, S. B. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.23.7148-7154.1994 · Cited by 76
The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon.
Kuhn, P., Weiche, B., Sturm, L., Sommer, E., Drepper, F., Warscheid, B., Sourjik, V., & Koch, H. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01167.x · Cited by 76
Self-citation
Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB
Lüke, I., Handford, J. I., Palmer, T., et al. (2009) · Archives of Microbiology · doi:10.1007/s00203-009-0516-5 · Cited by 76
Transport of proteins into chloroplasts. Requirements for the efficient import of two lumenal oxygen-evolving complex proteins into isolated thylakoids.
Mould, R. M., Shackleton, J. B., & Robinson, C. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47371-7 · Cited by 75
Functional genomic analysis of the Bacillus subtilis Tat pathway for protein secretion
van Dijl, J. M., Braun, P. G., Robinson, C., et al. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(02)00135-9 · Cited by 74
Search for Apoptotic Nucleases in Yeast
Qiu, J., Yoon, J., & Shen, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413547200 · Cited by 74
A single copy of SecYEG is sufficient for preprotein translocation.
Kedrov, A., Kusters, I., Krasnikov, V. V., & Driessen, A. J. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.314 · Cited by 74
SecA: a tale of two protomers
Sardis, M. F., & Economou, A. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07176.x · Cited by 73
Multiple Roles for the Twin Arginine Leader Sequence of Dimethyl Sulfoxide Reductase of Escherichia coli
Damaraju, S., Turner, R. J., Simala‐Grant, J. L., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909289199 · Cited by 72
Dual Topology of the Escherichia coli TatA Protein
Gouffi, K., Gérard, F., Santini, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313187200 · Cited by 72
Role of the Cytoplasmic Segments of Sec61α in the Ribosome-Binding and Translocation-Promoting Activities of the Sec61 Complex
Raden, D. L., Song, W., & Gilmore, R. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.1.53 · Cited by 72
The Entire N-Terminal Half of TatC is Involved in Twin-Arginine Precursor Binding
Holzapfel, E., Eisner, G., Alami, M., et al. (2007) · Biochemistry · doi:10.1021/bi062205b · Cited by 72
Local Translation and mRNA Trafficking in Axon Pathfinding
Yoon, B. C., Zivraj, K. H., & Holt, C. E. (2009) · Results and problems in cell differentiation · doi:10.1007/400_2009_5 · Cited by 71
Thylakoid targeting of Tat passenger proteins shows no ΔpH dependence in vivo
Finazzi, G., Chasen, C., Wollman, F.-A., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg081 · Cited by 71
SecA, a remarkable nanomachine
Küsters, I., & Driessen, A. J. M. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0681-y · Cited by 71
Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism
Walther, T. H., Gottselig, C., Grage, S. L., Wolf, M., Vargiu, A. V., Klein, M. J., Vollmer, S., Prock, S., Hartmann, M., Afonin, S., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.017 · Cited by 71
Clustering of C-Terminal Stromal Domains of Tha4 Homo-oligomers during Translocation by the Tat Protein Transport System
Dabney‐Smith, C., & Cline, K. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1189 · Cited by 71
Ligand crowding at a nascent signal sequence.
Eisner, G., Koch, H.-G., Beck, K., Brunner, J., & Müller, M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200306069 · Cited by 69
Self-citation
The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon.
Antonoaea, R., Fürst, M., Nishiyama, K.-I., & Müller, M. (2008) · Biochemistry · doi:10.1021/bi800233w · Cited by 69
Self-citation
Topological studies on the twin-arginine translocase component TatC
Behrendt, J. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.03.048 · Cited by 69
The Escherichia coli trigger factor
Hesterkamp, T., & Bukau, B. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00582-0 · Cited by 69
Biogenesis of MalF and the MalFGK2 Maltose Transport Complex in Escherichia coli Requires YidC
Wagner, S., Pop, O., Haan, G.-J., Baars, L., Koningstein, G. M., Klepsch, M. M., Genevaux, P., Luirink, J., & Gier, J. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801481200 · Cited by 69
Topological studies on the twin-arginine translocase component TatC
Behrendt, J., Standar, K., LindenstrauÃ, U., et al. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09548.x · Cited by 69
The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli.
Nishiyama, K., Mizushima, S.-I., & Tokuda, H. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50553-1 · Cited by 68
Membrane Binding of Twin Arginine Preproteins as an Early Step in Translocation
Shanmugham, A., Sang, H. W. W. F., Bollen, Y. J. M., et al. (2006) · Biochemistry · doi:10.1021/bi052188a · Cited by 68
Following the Path of a Twin-arginine Precursor along the TatABC Translocase of Escherichia coli
Panahandeh, S., Maurer, H. C., Moser, M. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804225200 · Cited by 68
Deregulation of the SecYEG Translocation Channel upon Removal of the Plug Domain
Maillard, A., Lalani, S., Silva, F., Belin, D., & Duong, F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610060200 · Cited by 68
Hydrophobically stabilized open state for the lateral gate of the Sec translocon
Zhang, B., & Miller, T. F. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914752107 · Cited by 68
The Chloroplast Tat Pathway Utilizes the Transmembrane Electric Potential as an Energy Source
Braun, N. A., Davis, A. W., & Theg, S. M. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.098731 · Cited by 68
Dissecting the Translocase and Integrase Functions of the Escherichia coli Secyeg Translocon
Koch, H., & Müller, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.3.689 · Cited by 68
Self-citation
Constructing the wonders of the bacterial world: biosynthesis of complex enzymes
Sargent, F. (2007) · Microbiology · doi:10.1099/mic.0.2006/004762-0 · Cited by 68
Potential receptor function of three homologous components, TatA, TatB and TatE, of the twin‐arginine signal sequence‐dependent metalloenzyme translocation pathway in Escherichia coli
Chanal, A., Santini, C., & Wu, L. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.01095.x · Cited by 68
Escherichia coli Twin Arginine (Tat) Mutant Translocases Possessing Relaxed Signal Peptide Recognition Specificities
Kreutzenbeck, P., Kröger, C., Lausberg, F., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610126200 · Cited by 67
Mapping Precursor-binding Site on TatC Subunit of Twin Arginine-specific Protein Translocase by Site-specific Photo Cross-linking
Zoufaly, S., Fröbel, J., Rose, P., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.343798 · Cited by 67
Characterization of the early steps of OE17 precursor transport by the thylakoid ΔpH/Tat machinery
Musser, S. M., & Theg, S. M. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01269.x · Cited by 66
Structural Determinants of Lateral Gate Opening in the Protein Translocon
Gumbart, J. C., & Schulten, K. (2007) · Biochemistry · doi:10.1021/bi700835d · Cited by 65
Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region.
Murphy, C., & Beckwith, J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.7.2557 · Cited by 65
SecA Supports a Constant Rate of Preprotein Translocation
Tomkiewicz, D., Nouwen, N. P., van Leeuwen, R., Tans, S. J., & Driessen, A. J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600205200 · Cited by 65
Pushing, pulling and trapping – Modes of motor protein supported protein translocation
Tomkiewicz, D., Nouwen, N. P., & Driessen, A. J. M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.015 · Cited by 65
The Oligomeric State and Arrangement of the Active Bacterial Translocon
Deville, K., Gold, V. A. M., Robson, A. D., Whitehouse, S., Sessions, R. B., Baldwin, S. A., Radford, S. E., & Collinson, I. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175638 · Cited by 64
Functional Tat Transport of Unstructured, Small, Hydrophilic Proteins
Richter, S., Lindenstrauß, U., Lücke, C., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703303200 · Cited by 63
Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA
Zimmer, J., & Rapoport, T. A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.10.024 · Cited by 63
Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB
Fröbel, J., Rose, P., Lausberg, F., Blümmel, A.-S., Freudl, R., & Müller, M. (2012) · Nature Communications · doi:10.1038/ncomms2308 · Cited by 63
Self-citation
A Cleavable N-Terminal Membrane Anchor is Involved in Membrane Binding of the Escherichia coli SRP Receptor
Weiche, B., Bürk, J., Angelini, S., Schiltz, E., Thumfart, J. O., & Koch, H. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.040 · Cited by 62
Self-citation
The Extraordinary Diversity of Bacterial Protein Secretion Mechanisms
Holland, I. B. (2010) · Methods in molecular biology · doi:10.1007/978-1-60327-412-8_1 · Cited by 62
Mitochondrial preprotein translocases as dynamic molecular machines
van der Laan, M., Rissler, M., & Rehling, P. (2006) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2006.00134.x · Cited by 61
Cysteine-scanning Mutagenesis and Disulfide Mapping Studies of the Conserved Domain of the Twin-arginine Translocase TatB Component
Lee, P. A., Orriss, G. L., Buchanan, G., Greene, N. P., Bond, P. J., Claire, P., Jack, R. L., Sansom, M. S. P., Berks, B. C., & Palmer, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607295200 · Cited by 60
An Essential Role for the DnaK Molecular Chaperone in Stabilizing Over-expressed Substrate Proteins of the Bacterial Twin-arginine Translocation Pathway
Pérez-Rodríguez, R., Fisher, A. C., Perlmutter, J. D., Hicks, M. G., Chanal, A., Santini, C., Wu, L., Palmer, T., & DeLisa, M. P. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.01.027 · Cited by 60
Product of a New Gene, syd, Functionally Interacts with SecY when Overproduced in Escherichia coli
Shimoike, T., Taura, T., Kihara, A., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5519 · Cited by 60
Early encounters of a nascent membrane protein
Houben, E. N. G., Zarivach, R., Oudega, B., & Luirink, J. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503035 · Cited by 60
YidC and SecY mediate membrane insertion of a Type I transmembrane domain.
Houben, E. N. G., Urbanus, M. L., van der Laan, M., ten Hagen-Jongman, C. M., Driessen, A. J. M., Brunner, J., Oudega, B., & Luirink, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205556200 · Cited by 60
Interconvertibility of lipid‐ and translocon‐bound forms of the bacterial Tat precursor pre‐SufI
Bageshwar, U. K., Whitaker, N., Liang, F., et al. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06862.x · Cited by 59
Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
Funes, S., Kauff, F., van der Sluis, E. O., Ott, M., & Herrmann, J. M. (2011) · Biological Chemistry · doi:10.1515/bc.2011.013 · Cited by 59
Long-Timescale Dynamics and Regulation of Sec-Facilitated Protein Translocation
Zhang, B., & Miller, T. F. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.08.039 · Cited by 59
Mapping of the SecA·SecY and SecA·SecG Interfaces by Site-directed in Vivo Photocross-linking
Das, S., & Oliver, D. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.182931 · Cited by 58
Stepwise evolution of the Sec machinery in Proteobacteria
van der Sluis, E. O., & Driessen, A. J. M. (2006) · Trends in Microbiology · doi:10.1016/j.tim.2006.01.009 · Cited by 58
The Twin-arginine Leader-binding Protein, DmsD, Interacts with the TatB and TatC Subunits of the Escherichia coli Twin-arginine Translocase
Papish, A. L., Ladner-Keay, C. L., & Turner, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301076200 · Cited by 58
Crystal Structure of the Major Periplasmic Domain of the Bacterial Membrane Protein Assembly Facilitator YidC
Oliver, D. C., & Paetzel, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708936200 · Cited by 58
Mapping the Sites of Interaction between SecY and SecE by Cysteine Scanning Mutagenesis
Veenendaal, A. K. J., van der Does, C., & Driessen, A. J. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103912200 · Cited by 58
Unassisted Membrane Insertion as the Initial Step in ΔpH/Tat-dependent Protein Transport
Hou, B., Frielingsdorf, S., & Klösgen, R. B. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.029 · Cited by 58
Competitive Binding of the SecA ATPase and Ribosomes to the SecYEG Translocon
Wu, Z. C., de Keyzer, J., Kedrov, A., & Driessen, A. J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.297911 · Cited by 58
Sequence-specific Binding of prePhoD to Soluble TatAd Indicates Protein-mediated Targeting of the Tat Export in Bacillus subtilis
Pop, O. I., Westermann, M., Volkmer, R., Schulz, D., Lemke, C., Schreiber, S., Gerlach, R. G., Wetzker, R., & Müller, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306516200 · Cited by 57
TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins
Maurer, H. C., Panahandeh, S., Jungkamp, A.-C., et al. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-07-0585 · Cited by 57
Subunit composition and in vivo substrate‐binding characteristics of Escherichia coli Tat protein complexes expressed at native levels
McDevitt, C. A., Buchanan, G., Sargent, F., et al. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05554.x · Cited by 57
The Bacterial Protein–Translocation Complex: SecYEG Dimers Associate with One or Two SecA Molecules
Tziatzios, C., Schubert, D., Lotz, M., Gundogan, D., Betz, H., Schägger, H., Haase, W., Duong, F., & Collinson, I. R. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.076 · Cited by 56
Cysteine Scanning Mutagenesis and Disulfide Mapping Studies of the TatA Component of the Bacterial Twin Arginine Translocase
Greene, N. P., Porcelli, I., Buchanan, G., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702972200 · Cited by 56
The Oligomeric Distribution of SecYEG is Altered by SecA and Translocation Ligands
Scheuring, J., Braun, N., Nothdurft, L., Stumpf, M., Veenendaal, A. K. J., Kol, S., van der Does, C., Driessen, A. J. M., & Weinkauf, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.09.058 · Cited by 56
A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli.
Deitermann, S., Sprie, G. S., & Koch, H.-G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509647200 · Cited by 56
Self-citation
Requirement of a Tha4-conserved Transmembrane Glutamate in Thylakoid Tat Translocase Assembly Revealed by Biochemical Complementation
Dabney‐Smith, C., Mori, H., & Cline, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307923200 · Cited by 56
TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli
Orriss, G. L., Tarry, M. J., Ize, B., et al. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.07.044 · Cited by 56
Stoichiometry for binding and transport by the twin arginine translocation system
Celedón, J. M., & Cline, K. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201201096 · Cited by 54
The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules
Matos, C. F. R. O., Robinson, C., & Cola, A. D. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.132 · Cited by 54
Molecular dissection of TatC defines critical regions essential for protein transport and a TatB–TatC contact site
Kneuper, H., Maldonado, B., Jäger, F., et al. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08151.x · Cited by 54
SecA, the Motor of the Secretion Machine, Binds Diverse Partners on One Interactive Surface
Cooper, D. B. J., Smith, V. F., Crane, J. M., Roth, H. C., Lilly, A. A., & Randall, L. L. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.049 · Cited by 53
Selective SecA Association with Signal Sequences in Ribosome-bound Nascent Chains
Karamyshev, A. L., & Johnson, A. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509100200 · Cited by 53
Two Cooperating Helices Constitute the Lipid-binding Domain of the Bacterial SRP Receptor
Braig, D., Baer, C. R., Thumfart, J. O., & Koch, H. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.061 · Cited by 53
Self-citation
Essential Cytoplasmic Domains in the Escherichia coli TatC Protein
Allen, S. C. H., Barrett, C. M. L., Ray, N., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109135200 · Cited by 53
Role of Vesicle‐Inducing Protein in Plastids 1 in cpTat transport at the thylakoid
Lo, S. M., & Theg, S. M. (2012) · The Plant Journal · doi:10.1111/j.1365-313x.2012.05020.x · Cited by 52
Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported
Ma, X., & Cline, K. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.44 · Cited by 52
Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work?
Mitra, K., Frank, J., & Driessen, A. J. M. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1166 · Cited by 50
Conserved Negative Charges in the Transmembrane Segments of Subunit K of the NADH:Ubiquinone Oxidoreductase Determine Its Dependence on YidC for Membrane Insertion
Price, C. E., & Driessen, A. J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.051128 · Cited by 50
The two membrane segments of leader peptidase partition one by one into the lipid bilayer via a Sec/YidC interface.
Houben, E. N. G., ten Hagen‐Jongman, C. M., Brunner, J., Oudega, B., & Luirink, J. (2004) · The EMBO Reports · doi:10.1038/sj.embor.7400261 · Cited by 50
pspA overexpression in Streptomyces lividans improves both Sec- and Tat-dependent protein secretion
Vrancken, K., Keersmaeker, S. D., Geukens, N., et al. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0571-7 · Cited by 50
Escherichia coli tatC Mutations that Suppress Defective Twin-Arginine Transporter Signal Peptides
Strauch, E., & Georgiou, G. N. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.09.050 · Cited by 50
Early Contacts between Substrate Proteins and TatA Translocase Component in Twin-arginine Translocation
Fröbel, J., Rose, P., & Müller, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.292565 · Cited by 49
Self-citation
Global Change of Gene Expression and Cell Physiology in YidC-DepletedEscherichia coli
Wang, P., Kühn, A., & Dalbey, R. (2010) · Journal of Bacteriology · doi:10.1128/jb.00484-09 · Cited by 49
Visualization of Distinct Entities of the SecYEG Translocon during Translocation and Integration of Bacterial Proteins
Boy, D., & Koch, H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-08-0886 · Cited by 49
Self-citation
Genetic Screen Yields Mutations in Genes Encoding All Known Components of the Escherichia coli Signal Recognition Particle Pathway
Tian, H., & Beckwith, J. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.1.111-118.2002 · Cited by 48
Complexes between Protein Export Chaperone SecB and SecA
Woodbury, R. L., Topping, T., Diamond, D. L., Suciu, D., Kumamoto, C. A., HARDY, S. J. S., & Randall, L. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002885200 · Cited by 48
Bacterial protein translocation requires only one copy of the SecY complex in vivo
Park, E., & Rapoport, T. A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201205140 · Cited by 48
Characterization of the Consequences of YidC Depletion on the Inner Membrane Proteome of E. coli Using 2D Blue Native/SDS-PAGE
Wickström, D., Wagner, S., Simonsson, P., Pop, O. I., Baars, L., Ytterberg, A. J., van Wijk, K. J., Luirink, J., & de Gier, J. L. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.068 · Cited by 47
Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex
Whitehouse, S., Gold, V. A. M., Robson, A. D., Allen, W. J., Sessions, R. B., & Collinson, I. R. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201205191 · Cited by 47
Precursors Bind to Specific Sites on Thylakoid Membranes prior to Transport on the Delta pH Protein Translocation System
Ma, X., & Cline, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10016 · Cited by 47
Signal peptide protection by specific chaperone
Genest, O., Seduk, F., Ilbert, M., Méjean, V., & Iobbi‐Nivol, C. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.11.107 · Cited by 46
Membrane Targeting of Ribosomes and Their Release Require Distinct and Separable Functions of FtsY
Bahari, L., Parlitz, R., Eitan, A., Stjepanović, G., Bochkareva, E. S., Sinning, I., & Bibi, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705429200 · Cited by 46
Projection Structure of yidC: A Conserved Mediator of Membrane Protein Assembly
Lotz, M., Haase, W., Kühlbrandt, W., & Collinson, I. R. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.089 · Cited by 46
The twin‐arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in Legionella pneumophila
Buck, E. D. J. D., Vranckx, L., Meyen, E., Maes, L., Vandersmissen, L., Anné, J., & Lammertyn, E. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.12.022 · Cited by 46
Co-operation between different targeting pathways during integration of a membrane protein.
Keller, R., de Keyzer, J., Driessen, A. J. M., & Palmer, T. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201204149 · Cited by 46
Escherichia coli TatA and TatB Proteins Have N-out, C-in Topology in Intact Cells
Koch, S., Fritsch, M. J., Buchanan, G., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.354555 · Cited by 46
SecY–SecY and SecY–SecG contacts revealed by site‐specific crosslinking
van der Sluis, E. O., Nouwen, N. P., & Driessen, A. J. M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03202-7 · Cited by 46
Dynamic Disulfide Scanning of the Membrane-inserting Pf3 Coat Protein Reveals Multiple YidC Substrate Contacts
Klenner, C., & Kühn, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.307223 · Cited by 45
Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle
Braig, D., Mircheva, M., Sachelaru, I., van der Sluis, E. O., Sturm, L., Beckmann, R., & Koch, H. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-02-0152 · Cited by 45
Self-citation
The Sec and Tat Protein Translocation Pathways in Chloroplasts
Cline, K. (2007) · The Enzymes · doi:10.1016/s1874-6047(07)25018-8 · Cited by 44
SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane
Sagara, K., Matsuyama, S., & Mizushima, S.-I. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.13.4111-4116.1994 · Cited by 44
Cysteine Scanning Mutagenesis and Topological Mapping of the Escherichia coli Twin-Arginine Translocase TatC Component
Punginelli, C., Maldonado, B., Grahl, S., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.00647-07 · Cited by 44
The Chloroplast Twin Arginine Transport (Tat) Component, Tha4, Undergoes Conformational Changes Leading to Tat Protein Transport
Aldridge, C., Storm, A. R., Cline, K., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.385666 · Cited by 43
SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature
Hanada, M., Nishiyama, K., & Tokuda, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00066-x · Cited by 42
An Escherichia coli twin‐arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment
San‐Miguel, M. A., Marrington, R., Rodger, P. M., et al. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03710.x · Cited by 42
A Periplasmic Fluorescent Reporter Protein and its Application in High-throughput Membrane Protein Topology Analysis
Jeong, K. J., Kawarasaki, Y., Gam, J., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.078 · Cited by 42
Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.
Mircheva, M., Boy, D., Weiche, B., Hucke, F., Graumann, P., & Koch, H.-G. (2009) · BMC Biology · doi:10.1186/1741-7007-7-76 · Cited by 42
Self-citation
In vivo studies of the role of SecA during protein export in Escherichia coli
Chun, S. Y., & Randall, L. L. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.14.4197-4203.1994 · Cited by 41
Visualizing Interactions along the Escherichia coli Twin-Arginine Translocation Pathway Using Protein Fragment Complementation
Kostecki, J. S., Li, H., Turner, R. J., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009225 · Cited by 41
Recombinant Expression of tatABC and tatAC Results in the Formation of Interacting Cytoplasmic TatA Tubes in Escherichia coli
Berthelmann, F., Mehner-Breitfeld, D., Richter, S., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707757200 · Cited by 40
Calorimetric analyses of the interaction between SecB and its ligands
Randall, L. L., Topping, T., Suciu, D., & HARDY, S. J. S. (1998) · Protein Science · doi:10.1002/pro.5560070514 · Cited by 40
The Conformation of a Signal Peptide Bound by Escherichia coli Preprotein Translocase SecA
Chou, Y.-T., & Gierasch, L. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507532200 · Cited by 40
Genetic Evidence for a Tight Cooperation of TatB and TatC during Productive Recognition of Twin-Arginine (Tat) Signal Peptides in Escherichia coli
Lausberg, F., Fleckenstein, S., Kreutzenbeck, P., Fröbel, J., Rose, P., Müller, M., & Freudl, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039867 · Cited by 39
Self-citation
Evidence for a loop mechanism of protein transport by the thylakoid Delta pH pathway
Fincher, V., McCaffery, M., & Cline, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00066-0 · Cited by 39
Environmental Salinity Determines the Specificity and Need for Tat-Dependent Secretion of the YwbN Protein in Bacillus subtilis
van der Ploeg, R., Mäder, U., Homuth, G., Schaffer, M., Denham, E. L., Monteferrante, C. G., Miethke, M., Marahiel, M. A., Harwood, C. R., Winter, T., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018140 · Cited by 39
The energetics of the chloroplast Tat protein transport pathway revisited
Theg, S. M., Cline, K., Finazzi, G., et al. (2005) · Trends in Plant Science · doi:10.1016/j.tplants.2005.02.001 · Cited by 39
A Facile Reporter System for the Experimental Identification of Twin-Arginine Translocation (Tat) Signal Peptides from All Kingdoms of Life
Widdick, D. A., Eijlander, R. T., van Dijl, J. M., Kuipers, O. P., & Palmer, T. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.002 · Cited by 39
The Tat Protein Export Pathway
Palmer, T., Sargent, F., & Berks, B. C. (2010) · EcoSal Plus · doi:10.1128/ecosalplus.4.3.2 · Cited by 39
Analysis of the Import of Carboxyl-Terminal Truncations of the 23-Kilodalton Subunit of the Oxygen-Evolving Complex Suggests That Its Structure Is an Important Determinant for Thylakoid Transport
Roffey, R. A., & Theg, S. M. (1996) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.4.1329 · Cited by 38
Structure, Binding, and Activity of Syd, a SecY-interacting Protein
Dalal, K., Nguyen, N. T., Alami, M., Tan, J. H., Moraes, T. F., Lee, W. C., Maurus, R., Sligar, S. G., Brayer, G. D., & Duong, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808305200 · Cited by 38
Differential effect of YidC depletion on the membrane proteome of Escherichia coli under aerobic and anaerobic growth conditions
Price, C. E., Otto, A., Fusetti, F., Becher, D., Hecker, M., & Driessen, A. J. M. (2010) · PROTEOMICS · doi:10.1002/pmic.201000284 · Cited by 38
The TatA Subunit ofEscherichia coliTwin-Arginine Translocase Has an N-in Topology
Chan, C. S., Zlomislic, M. R., Tieleman, D. P., et al. (2007) · Biochemistry · doi:10.1021/bi7005288 · Cited by 37
Evidence for variable rates of ribosome movement in Escherichia coli
Talkad, V. D., Schneider, E., & Kennell, D. E. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90015-2 · Cited by 37
Structure of TatA Paralog, TatE, Suggests a Structurally Homogeneous Form of Tat Protein Translocase That Transports Folded Proteins of Differing Diameter
Baglieri, J., Beck, D., Vasisht, N., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.326355 · Cited by 37
YidC, a Newly Defined Evolutionarily Conserved Protein, Mediates Membrane Protein Assembly in Bacteria
Chen, M., Xie, K., Jiang, F., Yi, L., & Dalbey, R. (2002) · Biological Chemistry · doi:10.1515/bc.2002.176 · Cited by 36
XthA (Exonuclease III) regulates loading of RecA onto DNA substrates in log phase Escherichia coli cells
Centore, R. C., Lestini, R., & Sandler, S. J. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.06026.x · Cited by 36
In vivo assessment of the Tat signal peptide specificity in Escherichia coli
Ize, B., Gérard, F., & Wu, L. (2002) · Archives of Microbiology · doi:10.1007/s00203-002-0488-1 · Cited by 35
The Core TatABC Complex of the Twin-arginine Translocase in Escherichia coli: TatC Drives Assembly Whereas TatA is Essential for Stability
Mangels, D., Mathers, J. E., Bolhuis, A., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.043 · Cited by 35
Affinity of TatCd for TatAd Elucidates Its Receptor Function in the Bacillus subtilis Twin Arginine Translocation (Tat) Translocase System
Schreiber, S., Stengel, R., Westermann, M., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513900200 · Cited by 35
Characterisation of Tat protein transport complexes carrying inactivating mutations
McDevitt, C. A., Hicks, M. G., Palmer, T., et al. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.038 · Cited by 35
The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding
Peterson, J. H., Woolhead, C. A., & Bernstein, H. D. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07325.x · Cited by 34
The TatBC complex formation suppresses a modular TatB‐multimerization in Escherichia coli
Behrendt, J., Lindenstrauß, U., & Brüser, T. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.07.045 · Cited by 34
The archaeal twin-arginine translocation pathway
Hutcheon, G. W., & Bolhuis, A. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310686 · Cited by 34
Membrane Protein TM Segments Are Retained at the Translocon during Integration until the Nascent Chain Cues FRET-Detected Release into Bulk Lipid
Hou, B., Lin, P.-J., & Johnson, A. E. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.023 · Cited by 34
Translation Elongation Regulates Substrate Selection by the Signal Recognition Particle
Zhang, D., & Shan, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.325001 · Cited by 34
Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in Tat‐mediated export
Jong, W. S. P., ten Hagen‐Jongman, C. M., Genevaux, P., et al. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04442.x · Cited by 34
Is there a twist in the Escherichia coli signal recognition particle pathway?
Bibi, E. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.09.004 · Cited by 34
Large-scale translocation reversal within the thylakoid Tat system in vivo
Cola, A. D., & Robinson, C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502067 · Cited by 33
Topology Inversion of SecG Is Essential for Cytosolic SecA-dependent Stimulation of Protein Translocation
Sugai, R., Takemae, K., Tokuda, H., & Nishiyama, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704716200 · Cited by 33
Functional analysis of TatA and TatB in Streptomyces lividans
Keersmaeker, S. D., Mellaert, L. V., Lammertyn, E., et al. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.07.165 · Cited by 33
Mutations in Subunits of the Escherichia coli Twin-arginine Translocase Block Function via Differing Effects on Translocation Activity or Tat Complex Structure
Barrett, C. M. L., Mangels, D., & Robinson, C. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.026 · Cited by 33
Ancestral and Derived Protein Import Pathways in the Mitochondrion of Reclinomonas americana
Tong, J., Doležal, P., Selkrig, J., Crawford, S., Simpson, A. G. B., Noinaj, N., Buchanan, S. K., Gabriel, K. P., & Lithgow, T. J. (2010) · Molecular Biology and Evolution · doi:10.1093/molbev/msq305 · Cited by 33
Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation
Nijeholt, J. A. L. A., Bulacu, M., Marrink, ‪. J., & Driessen, A. J. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.124636 · Cited by 33
Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins
Rocco, M. A., Waraho‐Zhmayev, D., & DeLisa, M. P. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210140109 · Cited by 32
Cross‐linked SecA dimers are not functional in protein translocation
Or, E., & Rapoport, T. A. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.083 · Cited by 32
The twin‐arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements
Barnett, J. P., van der Ploeg, R., Eijlander, R. T., et al. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06776.x · Cited by 32
Kinetics of Precursor Interactions with the Bacterial Tat Translocase Detected by Real-time FRET
Whitaker, N., Bageshwar, U. K., & Musser, S. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.324525 · Cited by 31
The TatAd component of the Bacillus subtilis twin-arginine protein transport system forms homo-multimeric complexes in its cytosolic and membrane embedded localisation
Westermann, M., Pop, O. I., Gerlach, R. G., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.018 · Cited by 30
Cotranslational Protein Folding within the Ribosome Tunnel Influences Trigger-Factor Recruitment
Lin, K.-F., Sun, C., Huang, Y., et al. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.04.048 · Cited by 30
A Stromal Pool of TatA Promotes Tat-dependent Protein Transport across the Thylakoid Membrane
Frielingsdorf, S., Jakob, M., & Klösgen, R. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806334200 · Cited by 30
Structural studies on a twin‐arginine signal sequence
Kipping, M., Lilie, H., Lindenstrauß, U., et al. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00804-4 · Cited by 29
Subunit Organization in the TatA Complex of the Twin Arginine Protein Translocase
White, G. F., Schermann, S. M., Bradley, J. M., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.065458 · Cited by 29
Unbalanced Charge Distribution as a Determinant for Dependence of a Subset of Escherichia coli Membrane Proteins on the Membrane Insertase YidC
Gray, A. N., Henderson-Frost, J. M., Boyd, D. H., Shirafi, S., Niki, H., & Goldberg, M. B. (2011) · mBio · doi:10.1128/mbio.00238-11 · Cited by 29
Enough is enough: TatA demand during Tat-dependent protein transport
Hauer, R. S., Schlesier, R., Heilmann, K., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.01.030 · Cited by 28
Membrane Protein Insertion of Variant MscL Proteins Occurs at YidC and SecYEG of Escherichia coli
Neugebauer, S. A., Baulig, A., Kühn, A., & Facey, S. J. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.046 · Cited by 28
SecA-dependence of the translocation of a large periplasmic loop in theEscherichia coliMalF inner membrane protein is a function of sequence context
Sääf, A. M., Andersson, H. M., Gafvelin, G., & von HEIJNE, G. (1995) · Molecular Membrane Biology · doi:10.3109/09687689509027509 · Cited by 28
Proton Transfer Limits Protein Translocation Rate by the Thylakoid ΔpH/Tat Machinery
Musser, S. M., & Theg, S. M. (2000) · Biochemistry · doi:10.1021/bi000115f · Cited by 27
High-Salinity Growth Conditions Promote Tat-Independent Secretion of Tat Substrates in Bacillus subtilis
van der Ploeg, R., Monteferrante, C. G., Piersma, S., Barnett, J. P., Kouwen, T. R. H. M., Robinson, C., & van Dijl, J. M. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.02093-12 · Cited by 27
Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin‐arginine translocase
Barrett, C. M. L., & Robinson, C. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04654.x · Cited by 26
Probing the Environment of Signal−Anchor Sequences during Topogenesis in the Endoplasmic Reticulum
Higy, M., Gander, S., & Spiess, M. (2005) · Biochemistry · doi:10.1021/bi047976z · Cited by 26
Direct Interaction between a Precursor Mature Domain and Transport Component Tha4 during Twin Arginine Transport of Chloroplasts
Pal, D., Fite, K., & Dabney‐Smith, C. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.207522 · Cited by 25
The Tat System for Membrane Translocation of Folded Proteins Recruits the Membrane-stabilizing Psp Machinery in Escherichia coli
Mehner-Breitfeld, D., Osadnik, H., Lünsdorf, H., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374983 · Cited by 25
Conservation of components of theEscherichia coliexport machinery in prokaryotes
Cook, H., & Tommassen, J. (1991) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1991.tb04660.x · Cited by 25
Direct Demonstration That Homotetrameric Chaperone SecB Undergoes a Dynamic Dimer-Tetramer Equilibrium
Topping, T., Woodbury, R. L., Diamond, D. L., HARDY, S. J. S., & Randall, L. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009584200 · Cited by 24
Prerequisites for Terminal Processing of Thylakoidal Tat Substrates
Frielingsdorf, S., & Klösgen, R. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702630200 · Cited by 24
Contributions of the Transmembrane Domain and a Key Acidic Motif to Assembly and Function of the TatA Complex
Warren, G. Z. L., Oates, J., Robinson, C., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.02.060 · Cited by 23
Genetic Evidence for a TatC Dimer at the Core of the Escherichia coli Twin Arginine (Tat) Protein Translocase
Maldonado, B., Buchanan, G., Müller, M. P., et al. (2011) · Microbial Physiology · doi:10.1159/000329076 · Cited by 23
Self-citation
Topologically Fixed SecG Is Fully Functional
van der Sluis, E. O., van der Vries, E., Berrelkamp, G., Nouwen, N. P., & Driessen, A. J. M. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.3.1188-1190.2006 · Cited by 22
Impairment of twin‐arginine‐dependent export by seemingly small alterations of substrate conformation
Maurer, H. C., Panahandeh, S., Moser, M. J., et al. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.038 · Cited by 21
Coupling between codon usage, translation and protein export in Escherichia coli
Zalucki, Y. M., Beacham, I. R., & Jennings, M. P. (2011) · Biotechnology Journal · doi:10.1002/biot.201000334 · Cited by 21
Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase
Maldonado, B., Kneuper, H., Buchanan, G., et al. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.016 · Cited by 21
Twin Arginine Translocation (Tat)-dependent Export in the Apparent Absence of TatABC or TatA Complexes Using Modified Escherichia coli TatA Subunits That Substitute for TatB
Barrett, C. M. L., Freudl, R., & Robinson, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704127200 · Cited by 20
Nearest Neighbor Analysis of the SecYEG Complex. 1. Identification of a SecY−SecG Interface
Satoh, Y., Matsumoto, G., Mori, H., & Ito, K. (2003) · Biochemistry · doi:10.1021/bi034331a · Cited by 20
Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport‐incompetent substrate
Alder, N. N., & Theg, S. M. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00231-x · Cited by 20
Multiple SecA Molecules Drive Protein Translocation across a Single Translocon with SecG Inversion
Morita, K., Tokuda, H., & Nishiyama, K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.301754 · Cited by 20
Roles of the C-Terminal End of SecY in Protein Translocation and Viability of Escherichia coli
Chiba, K., Mori, H., & Ito, K. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.8.2243-2250.2002 · Cited by 20
Substrate-Dependent Conformational Dynamics of the Escherichia coli Membrane Insertase YidC
Imhof, N., Kühn, A., & Gerken, U. (2011) · Biochemistry · doi:10.1021/bi1020293 · Cited by 19
Overlapping transport and chaperone‐binding functions within a bacterial twin‐arginine signal peptide
Grahl, S., Maillard, J., Spronk, C. A. E. M., Vuister, G. W., & Sargent, F. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08005.x · Cited by 17
The Thylakoid ΔpH/ΔΨ Are Not Required for the Initial Stages of Tat-dependent Protein Transport in Tobacco Protoplasts
Cola, A. D., Bailey, S., & Robinson, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509215200 · Cited by 17
Twin arginine translocation (Tat)-dependent protein transport: the passenger protein participates in the initial membrane binding step
Schlesier, R., & Klösgen, R. B. (2010) · Biological Chemistry · doi:10.1515/bc.2010.138 · Cited by 16
Twin-Arginine-Dependent Translocation of SufI in the Absence of Cytosolic Helper Proteins
Holzapfel, E., Moser, M. J., Schiltz, E., et al. (2009) · Biochemistry · doi:10.1021/bi900520d · Cited by 16
Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli
Chan, C. S., Haney, E. F., Vogel, H. J., & Turner, R. J. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.05.024 · Cited by 15
Molecular Machines Involved in Protein Transport across Cellular Membranes
van der Sluis, E. O., Nouwen, N. P., & Driessen, A. J. M. (2007) · The Enzymes · doi:10.1016/s1874-6047(07)x2500-9 · Cited by 12
A SecE Mutation That Modulates SecY-SecE Translocase Assembly, Identified as a Specific Suppressor of SecY Defects
Mori, H., Akiyama, Y., & Ito, K. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.3.948-956.2003 · Cited by 12
An inositol containing lipomannan fromPropionibacterium freudenreichii
Sutcliffe, I. C., & SHAW, N. (1989) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1989.tb03119.x · Cited by 12
Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of theEscherichia colimembrane-protein insertase YidC
Ravaud, S., Wild, K., & Sinning, I. (2008) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309108002364 · Cited by 5
RNA Localization Meets Wingless Signaling
Manseau, L. J. (2001) · Science s STKE · doi:10.1126/stke.2001.92.pe1 · Cited by 4

Research works printed but not linked: 2

de Cock, 1991, Conservation of components of the Escherichia coli export machinery in prokaryotes, FEMS Microbiol. Lett., 59, 249
Yen, 2002, Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system, Arch. Microbiol., 177, 441, 10.1007/s00203-002-0408-4 · DOI

Sorted by citations

The Sec translocon mediated protein transport in prokaryotes and eukaryotes.
Denks, K., Vogt, A., Sachelaru, I., Petriman, N.-A., Kudva, R., & Koch, H.-G. (2014) · Molecular Membrane Biology · doi:10.3109/09687688.2014.907455 · Cited by 170
Self-citation
Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane.
Castanié-Cornet, M.-P., Bruel, N., & Genevaux, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.007 · Cited by 129
Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon
Jomaa, A., Boehringer, D., Leibundgut, M., & Ban, N. (2016) · Nature Communications · doi:10.1038/ncomms10471 · Cited by 115
The Dynamic SecYEG Translocon
Oswald, J., Njenga, R., Natriashvili, A., Sarmah, P., & Koch, H.-G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.664241 · Cited by 88
Self-citation
Co-translational protein targeting in bacteria.
Steinberg, R., Knüpffer, L., Origi, A., Asti, R., & Koch, H.-G. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny095 · Cited by 81
Self-citation

See all 177

Authors: Kudva, R., Denks, K., Kuhn, P., Vogt, A., Müller, M., & Koch, H.-G.
Affiliations: University of Freiburg (DE)
Corresponding author: Müller, Matthias
Koch, Hans-Georg
ORCID: Kudva, Renuka
Denks, Kärt
Koch, Hans-Georg
Venue: Research in Microbiology
Publisher: Elsevier BV
Published: 2013-07
Volume: 164
Issue: 6
Pages: 505-534
ISSN: 0769-2609 (ISSN-L)
0923-2508
DOI: 10.1016/j.resmic.2013.03.016
OpenAlex: W1979649414
Cited by: 177
References: 402
Citations by year: 2026: 5 · 2025: 9 · 2024: 6 · 2023: 10 · 2022: 13 · 2021: 12 · 2020: 14 · 2019: 14 · 2018: 11 · 2017: 14 · 2016: 16 · 2015: 29 · 2014: 18 · 2013: 6
FWCI: 15.26
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3796 d)
Locations: Research in Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft (GSC‐4, FOR 967, SFB-746, FOR 929)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: protein translocation, Gram-negative bacteria, inner membrane, Sec translocon, Tat system, SecYEG translocon, signal recognition particle, SecA, molecular chaperones, membrane protein insertion, protein secretion, TatA, TATB, TatC
MeSH terms: Bacterial Proteins, Cell Membrane, Gram-Negative Bacteria, Protein Transport, Bacterial Secretion Systems

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks