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Cellular dynamics of the SecA ATPase at the single molecule level
In bacteria, the SecA ATPase provides the driving force for protein secretion via the SecYEG translocon. While the dynamic interplay between SecA and SecYEG in translocation is widely appreciated, it is not clear how SecA associates with the translocon in the crowded cellular environment. We use sup...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7809386/ https://www.ncbi.nlm.nih.gov/pubmed/33446830 http://dx.doi.org/10.1038/s41598-021-81081-2 |
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author | Seinen, Anne-Bart Spakman, Dian van Oijen, Antoine M. Driessen, Arnold J. M. |
author_facet | Seinen, Anne-Bart Spakman, Dian van Oijen, Antoine M. Driessen, Arnold J. M. |
author_sort | Seinen, Anne-Bart |
collection | PubMed |
description | In bacteria, the SecA ATPase provides the driving force for protein secretion via the SecYEG translocon. While the dynamic interplay between SecA and SecYEG in translocation is widely appreciated, it is not clear how SecA associates with the translocon in the crowded cellular environment. We use super-resolution microscopy to directly visualize the dynamics of SecA in Escherichia coli at the single-molecule level. We find that SecA is predominantly associated with and evenly distributed along the cytoplasmic membrane as a homodimer, with only a minor cytosolic fraction. SecA moves along the cell membrane as three distinct but interconvertible diffusional populations: (1) A state loosely associated with the membrane, (2) an integral membrane form, and (3) a temporarily immobile form. Disruption of the proton-motive-force, which is essential for protein secretion, re-localizes a significant portion of SecA to the cytoplasm and results in the transient location of SecA at specific locations at the membrane. The data support a model in which SecA diffuses along the membrane surface to gain access to the SecYEG translocon. |
format | Online Article Text |
id | pubmed-7809386 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-78093862021-01-15 Cellular dynamics of the SecA ATPase at the single molecule level Seinen, Anne-Bart Spakman, Dian van Oijen, Antoine M. Driessen, Arnold J. M. Sci Rep Article In bacteria, the SecA ATPase provides the driving force for protein secretion via the SecYEG translocon. While the dynamic interplay between SecA and SecYEG in translocation is widely appreciated, it is not clear how SecA associates with the translocon in the crowded cellular environment. We use super-resolution microscopy to directly visualize the dynamics of SecA in Escherichia coli at the single-molecule level. We find that SecA is predominantly associated with and evenly distributed along the cytoplasmic membrane as a homodimer, with only a minor cytosolic fraction. SecA moves along the cell membrane as three distinct but interconvertible diffusional populations: (1) A state loosely associated with the membrane, (2) an integral membrane form, and (3) a temporarily immobile form. Disruption of the proton-motive-force, which is essential for protein secretion, re-localizes a significant portion of SecA to the cytoplasm and results in the transient location of SecA at specific locations at the membrane. The data support a model in which SecA diffuses along the membrane surface to gain access to the SecYEG translocon. Nature Publishing Group UK 2021-01-14 /pmc/articles/PMC7809386/ /pubmed/33446830 http://dx.doi.org/10.1038/s41598-021-81081-2 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Seinen, Anne-Bart Spakman, Dian van Oijen, Antoine M. Driessen, Arnold J. M. Cellular dynamics of the SecA ATPase at the single molecule level |
title | Cellular dynamics of the SecA ATPase at the single molecule level |
title_full | Cellular dynamics of the SecA ATPase at the single molecule level |
title_fullStr | Cellular dynamics of the SecA ATPase at the single molecule level |
title_full_unstemmed | Cellular dynamics of the SecA ATPase at the single molecule level |
title_short | Cellular dynamics of the SecA ATPase at the single molecule level |
title_sort | cellular dynamics of the seca atpase at the single molecule level |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7809386/ https://www.ncbi.nlm.nih.gov/pubmed/33446830 http://dx.doi.org/10.1038/s41598-021-81081-2 |
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