Structure of a complex of the ATPase SecA and the protein-translocation channel.
Open accessAbstract
Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 ångström (A), obtained for components from Thermotoga maritima. One copy of SecA in an intermediate state of ATP hydrolysis is bound to one molecule of the SecY complex. Both partners undergo important conformational changes on interaction. The polypeptide-cross-linking domain of SecA makes a large conformational change that could capture the translocation substrate in a 'clamp'. Polypeptide movement through the SecY channel could be achieved by the motion of a 'two-helix finger' of SecA inside the cytoplasmic funnel of SecY, and by the coordinated tightening and widening of SecA's clamp above the SecY pore. SecA binding generates a 'window' at the lateral gate of the SecY channel and it displaces the plug domain, preparing the channel for signal sequence binding and channel opening.
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
Cites
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?
The Sec translocon in bacteria and eukaryotes is organized as a highly modular protein complex and multiple different entities have been structurally and biochemically characterized.
“The Sec translocon in bacteria and eukaryotes is organized as a highly modular protein complex and multiple different entities have been structurally and biochemically characterized (Zimmer et al., 2008; Boy and Koch, 2009; Frauenfeld et al., 2011; Denks et al., 2014; Komar et al., 2016; Kater et al., 2019).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Zimmer et al., 2008
SecYEG was found in heterotetrameric complexes with SecA or YidC, and as heterohexameric complexes with SecDFYajC or FtsY-SRP-RNCs.
“SecYEG was furthermore found in heterotetrameric complexes with SecA (Zimmer et al., 2008) or YidC (Boy and Koch, 2009; Sachelaru et al., 2017), and as heterohexameric complexes with SecDFYajC (Duong and Wickner, 1997) or FtsY-SRP-RNCs (Jomaa et al., 2017).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Zimmer et al., 2008
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works
Automated MAD and MIR structure solution
Terwilliger, T. C., & Berendzen, J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999000839 · Cited by 3,038 · see citing works
Improved Fourier coefficients for maps using phases from partial structures with errors
Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,885 · see citing works
Likelihood-enhanced fast translation functions
McCoy, A. J., Grosse‐Kunstleve, R. W., Storoni, L. C., & Read, R. J. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905001617 · Cited by 1,641 · see citing works
ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures
Landau, M., Mayrose, I., Rosenberg, Y., Glaser, F., Martz, E., Pupko, T., & Ben‐Tal, N. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki370 · Cited by 1,379 · see citing works
Version 1.2 of the Crystallography and NMR system
Brünger, A. T. (2007) · Nature Protocols · doi:10.1038/nprot.2007.406 · Cited by 1,335 · see citing works
X-ray structure of a protein-conducting channel
van den Berg, B., Clemons, W., Collinson, I. R., Modis, Y., Hartmann, E., Harrison, S. C., & Rapoport, T. A. (2003) · Nature · doi:10.1038/nature02218 · Cited by 1,252 · see citing works
Self-citationGlaser, F., Pupko, T., Paz, I., Bell, R. E., Shental-Bechor, D., Martz, E., & Ben‐Tal, N. (2002) · Bioinformatics · doi:10.1093/bioinformatics/19.1.163 · Cited by 1,237 · see citing works
Likelihood-enhanced fast rotation functions
Storoni, L. C., McCoy, A. J., & Read, R. J. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444903028956 · Cited by 1,177 · see citing works
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.
Rapoport, T. A. (2007) · Nature · doi:10.1038/nature06384 · Cited by 977 · see citing works
Self-citationVelankar, S. S., Soultanas, P., Dillingham, M. S., Subramanya, H. S., & Wigley, D. B. (1999) · Cell · doi:10.1016/s0092-8674(00)80716-3 · Cited by 785 · see citing works
Hartl, F.-U., Lecker, S., Schiebel, E., Hendrick, J. P., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90160-g · Cited by 562 · see citing works
Lill, R., Dowhan, W., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90742-w · Cited by 550 · see citing works
Economou, A., & Wickner, W. T. (1994) · Cell · doi:10.1016/s0092-8674(94)90582-7 · Cited by 520 · see citing works
Brundage, L., Hendrick, J. P., Schiebel, E., Driessen, A. J. M., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90111-q · Cited by 505 · see citing works
Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.
Gelis, I., Bonvin, A. M. J. J., Keramisanou, D., Koukaki, M., Gouridis, G., Karamanou, S., Economou, A., & Kalodimos, C. G. (2007) · Cell · doi:10.1016/j.cell.2007.09.039 · Cited by 433 · see citing works
Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane
Plath, K., Mothes, W., Wilkinson, B. M., Stirling, C. J., & Rapoport, T. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81738-9 · Cited by 345 · see citing works
Self-citationNucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA
Hunt, J. F., Weinkauf, S., Henry, L., Fak, J. J., McNicholas, P. M., Oliver, D. B., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1074424 · Cited by 270 · see citing works
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
VRIJE, T. D., de Swart, R. L., Dowhan, W., Tommassen, J., & KRUIJFF, B. D. (1988) · Nature · doi:10.1038/334173a0 · Cited by 266 · see citing works
Heinrich, S. U., Mothes, W., Brunner, J., & Rapoport, T. A. (2000) · Cell · doi:10.1016/s0092-8674(00)00028-3 · Cited by 264 · see citing works
Self-citationDensity modification for macromolecular phase improvement
Cowtan, K. D., & Zhang, K. Y. J. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(99)00008-5 · Cited by 260 · see citing works
Three-dimensional structure of the bacterial protein-translocation complex SecYEG
Breyton, C., Haase, W., Rapoport, T. A., Kühlbrandt, W., & Collinson, I. R. (2002) · Nature · doi:10.1038/nature00827 · Cited by 253 · see citing works
Self-citationPhase combination and cross validation in iterated density-modification calculations
Cowtan, K. D., & Main, P. (1996) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744499500761x · Cited by 247 · see citing works
Wang, J., Song, J., Franklin, M. C., Kamtekar, S., Im, Y. J., Rho, S., Seong, I. S., Lee, C. S., Chung, C. H., & Eom, S. H. (2001) · Structure · doi:10.1016/s0969-2126(01)00570-6 · Cited by 237 · see citing works
Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation
Hinnerwisch, J., Fenton, W. A., Furtak, K., Farr, G. W., & Horwich, A. L. (2005) · Cell · doi:10.1016/j.cell.2005.04.012 · Cited by 220 · see citing works
Inversion of the Membrane Topology of SecG Coupled with SecA-Dependent Preprotein Translocation
Nishiyama, K., Suzuki, T., & Tokuda, H. (1996) · Cell · doi:10.1016/s0092-8674(00)81083-1 · Cited by 217 · see citing works
Shiba, K., Ito, K., Yura, T., & Cerretti, D. P. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01859.x · Cited by 214 · see citing works
Akimaru, J., Matsuyama, S., Tokuda, H., & Mizushima, S.-I. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.15.6545 · Cited by 211 · see citing works
Central Pore Residues Mediate the p97/VCP Activity Required for ERAD
DeLaBarre, B., Christianson, J. C., Kopito, R. R., & Brünger, A. T. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.036 · Cited by 204 · see citing works
Martin, A., Baker, T. A., & Sauer, R. T. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.002 · Cited by 163 · see citing works
Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane
Or, E., Navon, A., & Rapoport, T. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf471 · Cited by 158 · see citing works
Self-citationSiddiqui, S. M., Sauer, R. T., & Baker, T. A. (2004) · Genes & Development · doi:10.1101/gad.1170304 · Cited by 154 · see citing works
A large conformational change of the translocation ATPase SecA
Osborne, A., Clemons, W., & Rapoport, T. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401742101 · Cited by 152 · see citing works
Self-citationNanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
Alami, M., Dalal, K., Lelj‐Garolla, B., Sligar, S. G., & Duong, F. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601661 · Cited by 151 · see citing works
Osborne, A. R., & Rapoport, T. A. (2007) · Cell · doi:10.1016/j.cell.2007.02.036 · Cited by 148 · see citing works
Self-citationA role for the two-helix finger of the SecA ATPase in protein translocation
Erlandson, K. J., Miller, S. B. M., Nam, Y., Osborne, A. R., Zimmer, J., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07439 · Cited by 140 · see citing works
Self-citationNeumann‐Haefelin, C., Schäfer, U., Müller, M., & Koch, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.23.6419 · Cited by 135 · see citing works
A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
Spyridoula Karamanou, A., Vrontou, E., Sianidis, G., Baud, C., Roos, T., Kühn, A., Politou, A. S., & Economou, A. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01686.x · Cited by 129 · see citing works
Investigating the SecY plug movement at the SecYEG translocation channel
Tam, P. C. K., Maillard, A., Chan, K. K.-Y., & Duong, F. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600804 · Cited by 129 · see citing works
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
Duong, F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg418 · Cited by 127 · see citing works
Harris, C. R., & Silhavy, T. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.11.3438-3444.1999 · Cited by 107 · see citing works
The Bacterial ATPase SecA Functions as a Monomer in Protein Translocation
Or, E., Boyd, D. H., Gon, S., Beckwith, J. R., & Rapoport, T. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413947200 · Cited by 104 · see citing works
Self-citationDimeric SecA is essential for protein translocation
Jilaveanu, L. B., Zito, C. R., & Oliver, D. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502774102 · Cited by 103 · see citing works
Zimmer, J., Li, W., & Rapoport, T. A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.044 · Cited by 86 · see citing works
Self-citationCovalently dimerized SecA is functional in protein translocation.
de Keyzer, J., van der Sluis, E. O., Spelbrink, R. E. J., Nijstad, N., de Kruijff, B., Nouwen, N., van der Does, C., & Driessen, A. J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506157200 · Cited by 82 · see citing works
Qi, H., & Bernstein, H. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8993 · Cited by 78 · see citing works
Considerations for the refinement of low-resolution crystal structures
DeLaBarre, B., & Brünger, A. T. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906012650 · Cited by 76 · see citing works
Structural determinants of SecB recognition by SecA in bacterial protein translocation
Zhou, J., & Xu, Z. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb980 · Cited by 72 · see citing works
Mori, H., & Ito, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081617398 · Cited by 68 · see citing works
Prinz, W. A., Spiess, C., Ehrmann, M., Schierle, C. F., & Beckwith, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00906.x · Cited by 66 · see citing works
Duong, F., & Wickner, W. (1998) · The EMBO Journal · doi:10.1093/emboj/17.3.696 · Cited by 65 · see citing works
Determining the Structure of an Unliganded and Fully Glycosylated SIV gp120 Envelope Glycoprotein
Chen, B., Vogan, E. M., Gong, H., Skehel, J. J., Wiley, D. C., & Harrison, S. C. (2005) · Structure · doi:10.1016/j.str.2004.12.004 · Cited by 64 · see citing works
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 · see citing works
Atomic Model of the E.coli Membrane-bound Protein Translocation Complex SecYEG
Bostina, M., Mohsin, B., Kühlbrandt, W., & Collinson, I. R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.005 · Cited by 51 · see citing works
Mitra, K., Frank, J., & Driessen, A. J. M. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1166 · Cited by 48 · see citing works
The Long α-Helix of SecA Is Important for the ATPase Coupling of Translocation
Mori, H., & Ito, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606906200 · Cited by 41 · see citing works
Isolation and analysis of dominant secA mutations in Escherichia coli
Jarosik, G. P., & Oliver, D. B. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.2.860-868.1991 · Cited by 25 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Mori, H., Shimizu, Y., & Ito, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204436200 · Cited by 11 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The Bacterial Cell EnvelopePreprint
Silhavy, T. J., Kahne, D. E., & Walker, S. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000414 · Cited by 3,834 · see citing works
Protein export through the bacterial Sec pathway
Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.161 · Cited by 447 · see citing works
Designer proteins: applications of genetic code expansion in cell biology
Davis, L., & Chin, J. W. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3286 · Cited by 349 · see citing works
Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes
Park, E., & Rapoport, T. A. (2012) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-050511-102312 · Cited by 348 · see citing works
Self-citationStructural and Mechanistic Insights into Protein Translocation
Rapoport, T. A., Li, L., & Park, E. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100616-060439 · Cited by 344 · see citing works
Self-citationStructure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution
Voorhees, R. M., Fernández, I. S., Scheres, S. H. W., & Hegde, R. S. (2014) · Cell · doi:10.1016/j.cell.2014.05.024 · Cited by 331 · see citing works
β-Barrel Membrane Protein Assembly by the Bam Complex
Hagan, C. L., Silhavy, T. J., & Kahne, D. E. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061408-144611 · Cited by 315 · see citing works
Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.
Frauenfeld, J., Gumbart, J., Sluis, E. O. V. D., Funes, S., Gartmann, M., Beatrix, B., Mielke, T., Berninghausen, O., Becker, T., Schulten, K., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2026 · Cited by 298 · see citing works
Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome
Becker, T., Bhushan, S., Jarasch, A., Armache, J., Funes, S., Jossinet, F., Gumbart, J. C., Mielke, T., Berninghausen, O., Schulten, K. J., et al. (2009) · Science · doi:10.1126/science.1178535 · Cited by 291 · see citing works
Membrane Protein Insertion at the Endoplasmic Reticulum
Shao, S., & Hegde, R. S. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154125 · Cited by 287 · see citing works
du Plessis, D. J. F., Nouwen, N. P., & Driessen, A. J. M. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.08.016 · Cited by 253 · see citing works
Structure of the Sec61 channel opened by a signal sequence
Voorhees, R. M., & Hegde, R. S. (2015) · Science · doi:10.1126/science.aad4992 · Cited by 241 · see citing works
Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory
Cournia, Z., Allen, T. W., Andricioaei, I., Antonny, B., Baum, D., Brannigan, G., Buchete, N.-V., Deckman, J. T., Delemotte, L., del Val, C., et al. (2015) · The Journal of Membrane Biology · doi:10.1007/s00232-015-9802-0 · Cited by 235 · see citing works
Structure and function of a membrane component SecDF that enhances protein export
Tsukazaki, T., Mori, H., Echizen, Y., Ishitani, R., Fukai, S., Tanaka, T., Perederina, A., Vassylyev, D. G., Kohno, T., Maturana, A. D., et al. (2011) · Nature · doi:10.1038/nature09980 · Cited by 219 · see citing works
Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion
Gogala, M., Becker, T. A., Beatrix, B., Armache, J., Barrio-Garcia, C., Berninghausen, O., & Beckmann, R. (2014) · Nature · doi:10.1038/nature12950 · Cited by 213 · see citing works
Co-translational targeting and translocation of proteins to the endoplasmic reticulum
Nyathi, Y., Wilkinson, B. M., & Pool, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.021 · Cited by 201 · see citing works
How Translocons Select Transmembrane Helices
White, S. H., & von HEIJNE, G. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125904 · Cited by 201 · see citing works
Structures of membrane proteins
Vinothkumar, K. R., & Henderson, R. A. (2010) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000041 · Cited by 198 · see citing works
Delivering proteins for export from the cytosol
Cross, B. C. S., Sinning, I., Luirink, J., & High, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2657 · Cited by 190 · see citing works
Structure of the native Sec61 protein-conducting channel
Pfeffer, S., Burbaum, L., Unverdorben, P., Pech, M., Chen, Y., Zimmermann, R., Beckmann, R., & Förster, F. G. (2015) · Nature Communications · doi:10.1038/ncomms9403 · Cited by 180 · see citing works
Crystal structure of a substrate-engaged SecY protein-translocation channel
Li, L., Park, E., Ling, J. J., Ingram, J. R., Ploegh, H. L., & Rapoport, T. A. (2016) · Nature · doi:10.1038/nature17163 · Cited by 180 · see citing works
Self-citationKudva, R., Denks, K., Kuhn, P., Vogt, A., Müller, M., & Koch, H.-G. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.03.016 · Cited by 177 · see citing works
Visualization of translation and protein biogenesis at the ER membrane
Gemmer, M., Chaillet, M. L., van Loenhout, J., Arenas, R. C., Vismpas, D., Gröllers‐Mulderij, M., Koh, F., Albanese, P., Scheltema, R. A., Howes, S. C., et al. (2023) · Nature · doi:10.1038/s41586-022-05638-5 · Cited by 176 · see citing works
Egea, P. F., & Stroud, R. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012556107 · Cited by 174 · see citing works
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 · see citing works
The action of cardiolipin on the bacterial translocon.
Gold, V. A. M., Robson, A., Bao, H., Romantsov, T., Duong, F., & Collinson, I. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914680107 · Cited by 168 · see citing works
Assembly of Bacterial Inner Membrane Proteins
Dalbey, R., Wang, P., & Kühn, A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060409-092524 · Cited by 166 · see citing works
The bacterial Sec-translocase: structure and mechanism
Nijeholt, J. A. L. A., & Driessen, A. J. M. (2012) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0201 · Cited by 164 · see citing works
Structure of the SecY channel during initiation of protein translocation
Park, E., Ménétret, J.-F., Gumbart, J. C., Ludtke, S. J., Li, W., Whynot, A., Rapoport, T. A., & Akey, C. W. (2014) · Nature · doi:10.1038/nature12720 · Cited by 148 · see citing works
Self-citationProtein Traffic in Gram-negative bacteria – how exported and secreted proteins find their way
Dalbey, R., & Kühn, A. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00327.x · Cited by 147 · see citing works
Structural insight into the mitochondrial protein import system.
Endo, T., Yamano, K., & Kawano, S. (2011) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2010.07.018 · Cited by 142 · see citing works
A role for the two-helix finger of the SecA ATPase in protein translocation
Erlandson, K. J., Miller, S. B. M., Nam, Y., Osborne, A. R., Zimmer, J., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07439 · Cited by 140 · see citing works
Self-citationBurmann, B. M., Wang, C., & Hiller, S. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2677 · Cited by 132 · see citing works
Structure of the post-translational protein translocation machinery of the ER membrane
Wu, X., Cabanos, C. S., & Rapoport, T. A. (2018) · Nature · doi:10.1038/s41586-018-0856-x · Cited by 123 · see citing works
Self-citationToward a structural understanding of co-translational protein translocation
Voorhees, R. M., & Hegde, R. S. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.04.009 · Cited by 122 · see citing works
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
Feld, G. K., Thoren, K. L., Kintzer, A. F., Sterling, H. J., Tang, I. I., Greenberg, S. G., Williams, E. R., & Krantz, B. A. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1923 · Cited by 120 · see citing works
Crystal structures of a polypeptide processing and secretion transporter
Lin, D. Y.-W., Huang, S., & Chen, J. (2015) · Nature · doi:10.1038/nature14623 · Cited by 118 · see citing works
Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip
Ponsero, A. J., Igbaria, A., Darch, M. A., Miled, S., Outten, C. E., Winther, J. R., Palais, G., D’Autréaux, B., Delaunay, A., & Tolédano, M. B. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.012 · Cited by 116 · see citing works
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 · see citing works
Regulation of the Protein-Conducting Channel by a Bound Ribosome
Gumbart, J. C., Trabuco, L. G., Schreiner, E., Villa, E., & Schulten, K. J. (2009) · Structure · doi:10.1016/j.str.2009.09.010 · Cited by 111 · see citing works
The Sec System: Protein Export in Escherichia coli
Crane, J. M., & Randall, L. (2017) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0002-2017 · Cited by 92 · see citing works
Bauer, B. W., Shemesh, T., Chen, Y., & Rapoport, T. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.063 · Cited by 109 · see citing works
Self-citationBeckwith, J. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.03.007 · Cited by 109 · see citing works
A clearer picture of the ER translocon complex
Gemmer, M., & Förster, F. G. (2020) · Journal of Cell Science · doi:10.1242/jcs.231340 · Cited by 106 · see citing works
Sachelaru, I., Petriman, N.-A., Kudva, R., Kuhn, P., Welte, T., Knapp, B. L., Drepper, F., Warscheid, B., & Koch, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.446583 · Cited by 105 · see citing works
Allen, W. J., Corey, R. A., Oatley, P., Sessions, R. B., Baldwin, S. A., Radford, S. E., Tuma, R., & Collinson, I. (2016) · eLife · doi:10.7554/elife.15598 · Cited by 103 · see citing works
The lateral gate of SecYEG opens during protein translocation.
du Plessis, D. J. F., Berrelkamp, G., Nouwen, N., & Driessen, A. J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901855200 · Cited by 102 · see citing works
Protein transport across and into cell membranes in bacteria and archaea
Yuan, J., Zweers, J. C., van Dijl, J. M., & Dalbey, R. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0160-x · Cited by 99 · see citing works
Membrane Insertion of Marginally Hydrophobic Transmembrane Helices Depends on Sequence Context
Hedin, L. E., Öjemalm, K., Bernsel, A., Hennerdal, A., Illergård, K., Enquist, K., Kauko, A., Cristóbal, S., von HEIJNE, G., Lerch, M., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.036 · Cited by 96 · see citing works
Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system
Wallden, K., Williams, R., Yan, J., Lian, P. W., Wang, L., Thalassinos, K., Orlova, E. V., & Waksman, G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201428109 · Cited by 92 · see citing works
SecA-mediated targeting and translocation of secretory proteins
Chatzi, K. E., Sardis, M. F., Economou, A., & Spyridoula Karamanou, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.02.014 · Cited by 90 · see citing works
Structure of the posttranslational Sec protein-translocation channel complex from yeast
Itskanov, S., & Park, E. (2018) · Science · doi:10.1126/science.aav6740 · Cited by 90 · see citing works
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 · see citing works
Emerging themes in SecA2-mediated protein export
Feltcher, M. E., & Braunstein, M. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2874 · Cited by 88 · see citing works
Hydrogen bond dynamics in membrane protein function
Bondar, A., & White, S. H. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.035 · Cited by 87 · see citing works
Biogenesis of inner membrane proteins in Escherichia coli
Luirink, J., Yu, Z. K., Wagner, S., & Gier, J. D. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.12.006 · Cited by 87 · see citing works
Rewiring translation – Genetic code expansion and its applications
Neumann, H. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.02.002 · Cited by 83 · see citing works
Protein Elongation, Co-translational Folding and Targeting
Rodnina, M. V., & Wintermeyer, W. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.022 · Cited by 82 · see citing works
Targeting and Insertion of Membrane Proteins
Kühn, A., Koch, H., & Dalbey, R. (2017) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0012-2016 · Cited by 80 · see citing works
An allosteric Sec61 inhibitor traps nascent transmembrane helices at the lateral gate
MacKinnon, A. L., Paavilainen, V. O., Sharma, A., Hegde, R. S., & Taunton, J. (2014) · eLife · doi:10.7554/elife.01483 · Cited by 78 · see citing works
The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.
Cranford-Smith, T., & Huber, D. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny093 · Cited by 77 · see citing works
Bacterial Signal Peptides- Navigating the Journey of Proteins
Kaushik, S., He, H., & Dalbey, R. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.933153 · Cited by 77 · see citing works
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 · see citing works
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 · see citing works
The unfolding story of anthrax toxin translocation
Thoren, K. L., & Krantz, B. A. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07614.x · Cited by 74 · see citing works
Breaking on through to the other side: protein export through the bacterial Sec system
Chatzi, K. E., Sardis, M. F., Spyridoula Karamanou, A., & Economou, A. (2012) · Biochemical Journal · doi:10.1042/bj20121227 · Cited by 74 · see citing works
Structure of the substrate-engaged SecA-SecY protein translocation machine
Ma, C., Wu, X., Sun, D., Park, E., Catipovic, M. A., Rapoport, T. A., Gao, N., & Li, L. (2019) · Nature Communications · doi:10.1038/s41467-019-10918-2 · Cited by 74 · see citing works
Self-citationLim, B., Miyazaki, R., Neher, S., Siegele, D. A., Ito, K., Walter, P., Akiyama, Y., Yura, T., & Gross, C. A. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001735 · Cited by 73 · see citing works
Sardis, M. F., & Economou, A. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07176.x · Cited by 73 · see citing works
Pisareva, T., Kwon, J. S., Oh, J., Kim, S.-H., Ge, C., Wieslander, Å., Choi, J., & Norling, B. (2011) · Journal of Proteome Research · doi:10.1021/pr200268r · Cited by 73 · see citing works
Bonardi, F., Halza, E., Walko, M., Du Plessis, F., Nouwen, N., Feringa, B. L., & Driessen, A. J. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101705108 · Cited by 72 · see citing works
Preprotein mature domains contain translocase targeting signals that are essential for secretion.
Chatzi, K. E., Sardis, M. F., Tsirigotaki, A., Koukaki, M., Šoštarić, N., Konijnenberg, A., Sobott, F., Kalodimos, C. G., Karamanou, S., & Economou, A. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201609022 · Cited by 72 · see citing works
The Blueprint of a Minimal Cell: MiniBacillus
Reuß, D. R., Commichau, F. M., Gundlach, J., Zhu, B., & Stülke, J. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00029-16 · Cited by 72 · see citing works
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 · see citing works
BrpA Is Involved in Regulation of Cell Envelope Stress Responses in Streptococcus mutans
Bitoun, J. P., Liao, S., Yao, X., Ahn, S., Isoda, R., Nguyen, A. H., Brady, L. J., Burne, R. A., Abranches, J., & Wen, Z. T. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.07823-11 · Cited by 70 · see citing works
Protein Translocation across the Rough Endoplasmic ReticulumPreprint
Mandon, E. C., Trueman, S. F., & Gilmore, R. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013342 · Cited by 70 · see citing works
Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.
Komar, J., Alvira, S., Schulze, R. J., Martin, R., Lycklama a Nijeholt, J. A., Lee, S. C., Dafforn, T. R., Deckers-Hebestreit, G., Berger, I., Schaffitzel, C., et al. (2016) · Biochemical Journal · doi:10.1042/bcj20160545 · Cited by 69 · see citing works
Visualization of a polytopic membrane protein during SecY-mediated membrane insertion
Bischoff, L., Wickles, S., Berninghausen, O., van der Sluis, E. O., & Beckmann, R. (2014) · Nature Communications · doi:10.1038/ncomms5103 · Cited by 69 · see citing works
Selective transport by SecA2: An expanding family of customized motor proteins
Bensing, B. A., Seepersaud, R., Yen, Y. T., & Sullam, P. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.019 · Cited by 68 · see citing works
Structure of the SecY complex unlocked by a preprotein mimic.
Hizlan, D., Robson, A., Whitehouse, S., Gold, V. A., Vonck, J., Mills, D., Kühlbrandt, W., & Collinson, I. (2012) · Cell Reports · doi:10.1016/j.celrep.2011.11.003 · Cited by 68 · see citing works
Tanaka, Y., Sugano, Y., Takemoto, M., Mori, T., Furukawa, A., Kusakizako, T., Kumazaki, K., Kashima, A., Ishitani, R., Sugita, Y., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.025 · Cited by 68 · see citing works
Corey, R. A., Pyle, E., Allen, W. J., Watkins, D. W., Casiraghi, M., Miroux, B., Aréchaga, I., Politis, A., & Collinson, I. R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721536115 · Cited by 68 · see citing works
Quaternary Structure of SecA in Solution and Bound to SecYEG Probed at the Single Molecule Level
Küsters, I., van den Bogaart, G., Kedrov, A., Krasnikov, V. V., Fulyani, F., Poolman, B., & Driessen, A. J. M. (2011) · Structure · doi:10.1016/j.str.2010.12.016 · Cited by 68 · see citing works
Free-energy cost for translocon-assisted insertion of membrane proteins
Gumbart, J. C., Chipot, C. J., & Schulten, K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012758108 · Cited by 67 · see citing works
Petriman, N.-A., Jauß, B., Hufnagel, A., Franz, L., Sachelaru, I., Drepper, F., Warscheid, B., & Koch, H.-G. (2018) · Scientific Reports · doi:10.1038/s41598-017-19019-w · Cited by 66 · see citing works
Stepwise gating of the Sec61 protein-conducting channel by Sec63 and Sec62
Itskanov, S., Kuo, K. M., Gumbart, J. C., & Park, E. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00541-x · Cited by 65 · see citing works
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 · see citing works
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 64 · see citing works
Mapping polypeptide interactions of the SecA ATPase during translocation
Bauer, B. W., & Rapoport, T. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910550106 · Cited by 63 · see citing works
Self-citationConformational 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 · see citing works
Self-citationChannel crossing: how are proteins shipped across the bacterial plasma membrane?
Collinson, I. R., Corey, R. A., & Allen, W. J. (2015) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2015.0025 · Cited by 63 · see citing works
Mechanism of Protein Translocation by the Sec61 Translocon ComplexPreprint
Itskanov, S., & Park, E. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041250 · Cited by 63 · see citing works
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Bonardi, F., London, G., Nouwen, N. P., Feringa, B. L., & Driessen, A. J. M. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201002243 · Cited by 62 · see citing works
Antibiotic targeting of the bacterial secretory pathway
Smitha Rao, C. V., Waelheyns, E. D., Economou, A., & Anné, J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.02.004 · Cited by 61 · see citing works
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 61 · see citing works
Biogenesis of membrane bound respiratory complexes in Escherichia coli
Price, C. E., & Driessen, A. J. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.01.019 · Cited by 61 · see citing works
Wang, Y., Wang, R., Jin, F., Liu, Y., Yu, J., Fu, X., & Chang, Z. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.710715 · Cited by 60 · see citing works
Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion
Ge, Y., Draycheva, A., Bornemann, T., Rodnina, M. V., & Wintermeyer, W. (2014) · Nature Communications · doi:10.1038/ncomms6263 · Cited by 60 · see citing works
Mechanical architecture and folding of E. coli type 1 pilus domains
Alonso-Caballero, Á., Schönfelder, J., Poly, S., Corsetti, F., Sancho, D. D., Artacho, E., & Pérez‐Jiménez, R. (2018) · Nature Communications · doi:10.1038/s41467-018-05107-6 · Cited by 60 · see citing works
The first low μM SecA inhibitors
Chen, W., Huang, Y., Gundala, S. R., Yang, H., Li, M., Tai, P. C., & Wang, B. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.12.074 · Cited by 59 · see citing works
- Authors
- Zimmer, J., Nam, Y., & Rapoport, T. A.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Rapoport, Tom A.
- Venue
- Nature
- Published
- 2008-10
- Volume
- 455
- Issue
- 7215
- Pages
- 936-943
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7164768
- OpenAlex
- W1968636401
- Cited by
- 459
- References
- 64
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 12 · 2023: 8 · 2022: 20 · 2021: 16 · 2020: 27 · 2019: 41 · 2018: 24 · 2017: 20 · 2016: 30 · 2015: 29 · 2014: 29 · 2013: 27 · 2012: 41
- FWCI
- 23.38
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (R01GM052586)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- SecA ATPase, protein translocation, crystal structure, Thermotoga maritima, conformational change, channel gating, bacterial protein secretion
- MeSH terms
- SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Adenosine Triphosphate, Bacillus subtilis, Bacterial Proteins, Hydrolysis, Models, Biological, Models, Molecular, Movement, Protein Binding, Protein Conformation, Structure-Activity Relationship, Crystallography, X-Ray, Thermotoga maritima, Protein Transport, Protein Sorting Signals, Membrane Transport Proteins, Multiprotein Complexes
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