Cellular dynamics of the SecA ATPase at the single molecule level

Abstract 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. W...

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Autores principales:	Anne-Bart Seinen, Dian Spakman, Antoine M. van Oijen, Arnold J. M. Driessen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1c394121d58f465a8a690efb6cc8ef7e
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spelling	oai:doaj.org-article:1c394121d58f465a8a690efb6cc8ef7e2021-12-02T15:23:10ZCellular dynamics of the SecA ATPase at the single molecule level10.1038/s41598-021-81081-22045-2322https://doaj.org/article/1c394121d58f465a8a690efb6cc8ef7e2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-81081-2https://doaj.org/toc/2045-2322Abstract 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.Anne-Bart SeinenDian SpakmanAntoine M. van OijenArnold J. M. DriessenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anne-Bart Seinen Dian Spakman Antoine M. van Oijen Arnold J. M. Driessen Cellular dynamics of the SecA ATPase at the single molecule level
description	Abstract 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	article
author	Anne-Bart Seinen Dian Spakman Antoine M. van Oijen Arnold J. M. Driessen
author_facet	Anne-Bart Seinen Dian Spakman Antoine M. van Oijen Arnold J. M. Driessen
author_sort	Anne-Bart Seinen
title	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_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_sort	cellular dynamics of the seca atpase at the single molecule level
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1c394121d58f465a8a690efb6cc8ef7e
work_keys_str_mv	AT annebartseinen cellulardynamicsofthesecaatpaseatthesinglemoleculelevel AT dianspakman cellulardynamicsofthesecaatpaseatthesinglemoleculelevel AT antoinemvanoijen cellulardynamicsofthesecaatpaseatthesinglemoleculelevel AT arnoldjmdriessen cellulardynamicsofthesecaatpaseatthesinglemoleculelevel
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Cellular dynamics of the SecA ATPase at the single molecule level

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