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Driving Forces of Translocation Through Bacterial Translocon SecYEG

This review focusses on the energetics of protein translocation via the Sec translocation machinery. First we complement structural data about SecYEG’s conformational rearrangements by insight obtained from functional assays. These include measurements of SecYEG permeability that allow assessment of...

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Autores principales: Knyazev, Denis G., Kuttner, Roland, Zimmermann, Mirjam, Sobakinskaya, Ekaterina, Pohl, Peter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6028853/
https://www.ncbi.nlm.nih.gov/pubmed/29330604
http://dx.doi.org/10.1007/s00232-017-0012-9
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author Knyazev, Denis G.
Kuttner, Roland
Zimmermann, Mirjam
Sobakinskaya, Ekaterina
Pohl, Peter
author_facet Knyazev, Denis G.
Kuttner, Roland
Zimmermann, Mirjam
Sobakinskaya, Ekaterina
Pohl, Peter
author_sort Knyazev, Denis G.
collection PubMed
description This review focusses on the energetics of protein translocation via the Sec translocation machinery. First we complement structural data about SecYEG’s conformational rearrangements by insight obtained from functional assays. These include measurements of SecYEG permeability that allow assessment of channel gating by ligand binding and membrane voltage. Second we will discuss the power stroke and Brownian ratcheting models of substrate translocation and the role that the two models assign to the putative driving forces: (i) ATP (SecA) and GTP (ribosome) hydrolysis, (ii) interaction with accessory proteins, (iii) membrane partitioning and folding, (iv) proton motive force (PMF), and (v) entropic contributions. Our analysis underlines how important energized membranes are for unravelling the translocation mechanism in future experiments.
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spelling pubmed-60288532018-07-23 Driving Forces of Translocation Through Bacterial Translocon SecYEG Knyazev, Denis G. Kuttner, Roland Zimmermann, Mirjam Sobakinskaya, Ekaterina Pohl, Peter J Membr Biol Article This review focusses on the energetics of protein translocation via the Sec translocation machinery. First we complement structural data about SecYEG’s conformational rearrangements by insight obtained from functional assays. These include measurements of SecYEG permeability that allow assessment of channel gating by ligand binding and membrane voltage. Second we will discuss the power stroke and Brownian ratcheting models of substrate translocation and the role that the two models assign to the putative driving forces: (i) ATP (SecA) and GTP (ribosome) hydrolysis, (ii) interaction with accessory proteins, (iii) membrane partitioning and folding, (iv) proton motive force (PMF), and (v) entropic contributions. Our analysis underlines how important energized membranes are for unravelling the translocation mechanism in future experiments. Springer US 2018-01-12 2018 /pmc/articles/PMC6028853/ /pubmed/29330604 http://dx.doi.org/10.1007/s00232-017-0012-9 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Article
Knyazev, Denis G.
Kuttner, Roland
Zimmermann, Mirjam
Sobakinskaya, Ekaterina
Pohl, Peter
Driving Forces of Translocation Through Bacterial Translocon SecYEG
title Driving Forces of Translocation Through Bacterial Translocon SecYEG
title_full Driving Forces of Translocation Through Bacterial Translocon SecYEG
title_fullStr Driving Forces of Translocation Through Bacterial Translocon SecYEG
title_full_unstemmed Driving Forces of Translocation Through Bacterial Translocon SecYEG
title_short Driving Forces of Translocation Through Bacterial Translocon SecYEG
title_sort driving forces of translocation through bacterial translocon secyeg
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6028853/
https://www.ncbi.nlm.nih.gov/pubmed/29330604
http://dx.doi.org/10.1007/s00232-017-0012-9
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