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. 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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Seinen AB,Spakman D,van Oijen AM,Driessen AJM

doi

10.1038/s41598-021-81081-2

subject

Has Abstract

pub_date

2021-01-14 00:00:00

pages

1433

issue

1

issn

2045-2322

pii

10.1038/s41598-021-81081-2

journal_volume

11

pub_type

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