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Dynamic action of the Sec machinery during initiation, protein translocation and termination

T. Fessl, D. Watkins, P. Oatley, WJ. Allen, RA. Corey, J. Horne, SA. Baldwin, SE. Radford, I. Collinson, R. Tuma,

. 2018 ; 7 (-) : . [pub] 20180607

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc19028395

Grantová podpora
BB/M003604/I Biotechnology and Biological Sciences Research Council - United Kingdom
BB/M011151/1 Biotechnology and Biological Sciences Research Council - United Kingdom
BBSRC South West Bioscience Doctoral Training Partnership Biotechnology and Biological Sciences Research Council - United Kingdom
BB/I006737/1 Biotechnology and Biological Sciences Research Council - United Kingdom
BB/I008675/1 Biotechnology and Biological Sciences Research Council - United Kingdom
BB/N017307/1 Biotechnology and Biological Sciences Research Council - United Kingdom
104632 Wellcome Trust - United Kingdom
Wellcome Trust - United Kingdom
BB/N015126/1 Biotechnology and Biological Sciences Research Council - United Kingdom

Protein translocation across cell membranes is a ubiquitous process required for protein secretion and membrane protein insertion. In bacteria, this is mostly mediated by the conserved SecYEG complex, driven through rounds of ATP hydrolysis by the cytoplasmic SecA, and the trans-membrane proton motive force. We have used single molecule techniques to explore SecY pore dynamics on multiple timescales in order to dissect the complex reaction pathway. The results show that SecA, both the signal sequence and mature components of the pre-protein, and ATP hydrolysis each have important and specific roles in channel unlocking, opening and priming for transport. After channel opening, translocation proceeds in two phases: a slow phase independent of substrate length, and a length-dependent transport phase with an intrinsic translocation rate of ~40 amino acids per second for the proOmpA substrate. Broad translocation rate distributions reflect the stochastic nature of polypeptide transport.

Citace poskytuje Crossref.org

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$a Fessl, Tomas $u Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom. School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom. Faculty of Science, University of South Bohemia, Ceske Budejovice, Czech Republic.
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$a Protein translocation across cell membranes is a ubiquitous process required for protein secretion and membrane protein insertion. In bacteria, this is mostly mediated by the conserved SecYEG complex, driven through rounds of ATP hydrolysis by the cytoplasmic SecA, and the trans-membrane proton motive force. We have used single molecule techniques to explore SecY pore dynamics on multiple timescales in order to dissect the complex reaction pathway. The results show that SecA, both the signal sequence and mature components of the pre-protein, and ATP hydrolysis each have important and specific roles in channel unlocking, opening and priming for transport. After channel opening, translocation proceeds in two phases: a slow phase independent of substrate length, and a length-dependent transport phase with an intrinsic translocation rate of ~40 amino acids per second for the proOmpA substrate. Broad translocation rate distributions reflect the stochastic nature of polypeptide transport.
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$a Watkins, Daniel $u School of Biochemistry, University of Bristol, Bristol, United Kingdom.
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