Preprotein-controlled catalysis in the helicase motor of SecA.

The DEAD-box protein family of RNA helicases

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Crystal Structures of Complexes of PcrA DNA Helicase with a DNA Substrate Indicate an Inchworm Mechanism

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Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa

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Helicase structure and mechanism

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The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane

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The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins

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SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion

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ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

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PROTEIN TRANSLOCATION BY THE SEC61/SECY CHANNEL

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Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase

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Structural Analysis of DNA Replication Fork Reversal by RecG

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Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA

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Two distinct ATP‐binding domains are needed to promote protein export by Escherichia coli SecA ATPase

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Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair

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Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor.

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The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases

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Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

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Structural basis for the enhancement of eIF4A helicase activity by eIF4GPreprint

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Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane

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A large conformational change of the translocation ATPase SecA

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Structure of Dimeric SecA, the Escherichia coli Preprotein Translocase Motor

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The protein-conducting channel SecYEG

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A molecular switch in SecA protein couples ATP hydrolysis to protein translocation

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Structure and function of SecA, the preprotein translocase nanomotor

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Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase

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Cross‐talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function

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Structural basis for DNA recognition and processing by UvrB

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Topology of the Integral Membrane Form of Escherichia coli SecA Protein Reveals Multiple Periplasmically Exposed Regions and Modulation by ATP Binding

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Phospholipid-induced Monomerization and Signal-peptide-induced Oligomerization of SecA

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Identification of the Preprotein Binding Domain of SecA

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A DEAD Protein that Activates Intron Self-Splicing without Unwinding RNA

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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 · see citing works

Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation

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Crystal Structure of M. tuberculosis SecA, A Preprotein Translocating ATPase

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Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein

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Allosteric Communication between Signal Peptides and the SecA Protein DEAD Motor ATPase Domain

Baud, C., Spyridoula Karamanou, A., Sianidis, G., Vrontou, E., Politou, A. S., & Economou, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200047200 · Cited by 52 · see citing works

Nucleotide Exchange from the High-Affinity ATP-Binding Site in SecA Is the Rate-Limiting Step in the ATPase Cycle of the Soluble Enzyme and Occurs through a Specialized Conformational State

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Global Co-ordination of Protein Translocation by the SecA IRA1 Switch

Vrontou, E., Spyridoula Karamanou, A., Baud, C., Sianidis, G., & Economou, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401008200 · Cited by 51 · see citing works

Selective Photoaffinity Labeling Identifies the Signal Peptide Binding Domain on SecA

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The Long α-Helix of SecA Is Important for the ATPase Coupling of Translocation

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The Conformation of a Signal Peptide Bound by Escherichia coli Preprotein Translocase SecA

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Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation

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Regulation of Escherichia coli secA mRNA translation by a secretion-responsive element

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In Vivo Membrane Topology of Escherichia coli SecA ATPase Reveals Extensive Periplasmic Exposure of Multiple Functionally Important Domains Clustering on One Face of SecA

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Functionally Significant Mobile Regions of Escherichia coli SecA ATPase Identified by NMR

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Helicase Motif III in SecA is essential for coupling preprotein binding to translocation ATPase

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Isolation and analysis of dominant secA mutations in Escherichia coli

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Disorder breathes life into a DEAD motor

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Purification of a functional mature region from a SecA-dependent preprotein

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Protein Translocation Across the Bacterial Cytoplasmic Membrane

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Protein export through the bacterial Sec pathway

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Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.

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Bacterial protein secretion through the translocase nanomachine

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The Sec translocase

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Conformational transition of Sec machinery inferred from bacterial SecYE structures

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Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function

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The bacterial Sec-translocase: structure and mechanism

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Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion

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Signal peptides are allosteric activators of the protein translocase

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The Sec System: Protein Export in Escherichia coli

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The Dynamic SecYEG Translocon

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SecA-mediated targeting and translocation of secretory proteins

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Breaking on through to the other side: protein export through the bacterial Sec system

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Selective transport by SecA2: An expanding family of customized motor proteins

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SecA: a tale of two protomers

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The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY

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SecA, a remarkable nanomachine

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Energy transduction in protein transport and the ATP hydrolytic cycle of SecA

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SecYEG activates GTPases to drive the completion of cotranslational protein targeting

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Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function

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Traffic Jam at the Bacterial Sec Translocase: Targeting the SecA Nanomotor by Small-Molecule Inhibitors

Segers, K., & Anné, J. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.04.007 · Cited by 47 · see citing works

Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex

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Large-scale production of a thermostable Rhodothermus marinus cellulase by heterologous secretion from Streptomyces lividans

Hamed, M. B., Spyridoula Karamanou, A., Ólafsdóttir, S., et al. (2017) · Microbial Cell Factories · doi:10.1186/s12934-017-0847-x · Cited by 48 · see citing works

Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists

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Structure and Mechanisms of SF2 DNA Helicases

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SecA: A Potential Antimicrobial Target

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Recent developments of bio-molecular motors as on-chip devices using single molecule techniques

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Molecular mimicry of SecA and signal recognition particle binding to the bacterial ribosome.

Knüpffer, L., Fehrenbach, C., Denks, K., Erichsen, V., Petriman, N.-A., & Koch, H.-G. (2019) · mBio · doi:10.1128/mbio.01317-19 · Cited by 28 · see citing works

Characterization of Streptococcus gordonii SecA2 as a Paralogue of SecA

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Preprotein Conformational Dynamics Drive Bivalent Translocase Docking and Secretion

Sardis, M. F., Tsirigotaki, A., Chatzi, K. E., Portaliou, A. G., Gouridis, G., Spyridoula Karamanou, A., & Economou, A. (2017) · Structure · doi:10.1016/j.str.2017.05.012 · Cited by 25 · see citing works

ABCH2 transporter mediates deltamethrin uptake and toxicity in the malaria vector Anopheles coluzzii

Kefi, M., Balabanidou, V., Sarafoglou, C., Charamis, J., Lycett, G. J., Ranson, H., Gouridis, G., & VONTAS, J. G. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011226 · Cited by 24 · see citing works

Assembly of the translocase motor onto the preprotein‐conducting channel

Spyridoula Karamanou, A., Bariami, V., Papanikou, E., Kalodimos, C. G., & Economou, A. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06402.x · Cited by 24 · see citing works

Using Graphs of Dynamic Hydrogen-Bond Networks To Dissect Conformational Coupling in a Protein Motor

Karathanou, K., & Bondar, A. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00979 · Cited by 22 · see citing works

Supplementary Materials and Methods

Groenendijk, F. H., Zwart, W. T., Floore, A. N., Akbari, S., & Bernards, R. (2013) · Cited by 22 · see citing works

In Vitro Assays to Analyze Translocation of the Model Secretory Preprotein Alkaline Phosphatase

Gouridis, G., Spyridoula Karamanou, A., Koukaki, M., & Economou, A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60327-412-8_10 · Cited by 20 · see citing works

A nexus of intrinsic dynamics underlies translocase priming

Krishnamurthy, S., Eleftheriadis, N., Karathanou, K., Smit, J. H., Portaliou, A. G., Chatzi, K. E., Spyridoula Karamanou, A., Bondar, A., Gouridis, G., & Economou, A. (2021) · Structure · doi:10.1016/j.str.2021.03.015 · Cited by 18 · see citing works

Large conformational changes of a highly dynamic pre-protein binding domain in SecA

Ernst, I., Haase, M., Ernst, S., Yuan, S., Kühn, A., & Leptihn, S. (2018) · Communications Biology · doi:10.1038/s42003-018-0133-4 · Cited by 17 · see citing works

The Preprotein Binding Domain of SecA Displays Intrinsic Rotational Dynamics

Vandenberk, N., Spyridoula Karamanou, A., Portaliou, A. G., Zorzini, V., Hofkens, J., Hendrix, J., & Economou, A. (2018) · Structure · doi:10.1016/j.str.2018.10.006 · Cited by 17 · see citing works

Inner Membrane Translocases and Insertases

Geyter, J. D., Smets, D., Spyridoula Karamanou, A., & Economou, A. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-18768-2_11 · Cited by 13 · see citing works

Fates of Sec, Tat, and YidC Translocases in Mitochondria and Other Eukaryotic Compartments

Petrů, M., Dohnálek, V., Füssy, Z., & Doležal, P. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab253 · Cited by 15 · see citing works

Preproteins couple the intrinsic dynamics of SecA to its ATPase cycle to translocate via a catch and release mechanism

Krishnamurthy, S., Sardis, M. F., Eleftheriadis, N., Chatzi, K. E., Smit, J. H., Karathanou, K., Gouridis, G., Portaliou, A. G., Bondar, A., Spyridoula Karamanou, A., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110346 · Cited by 14 · see citing works

Mechanism of conformational coupling in SecA: Key role of hydrogen-bonding networks and water interactions

Milenkovic, S., & Bondar, A. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.11.010 · Cited by 13 · see citing works

ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase

Kim, D. M., Zheng, H., Huang, Y. J., Montelione, G. T., & Hunt, J. F. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306361q · Cited by 13 · see citing works

Motions of the SecA protein motor bound to signal peptide: Insights from molecular dynamics simulations

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Single-Molecule Studies on the Protein Translocon

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