Stabilization of SecA ATPase by the Primary Cytoplasmic Salt of Escherichia Coli

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2019 Apr 11

PMID 30968480

Citations 4

Authors

Guillaume Roussel

Eric Lindner

Stephen H White

Affiliations

Soon will be listed here.

Abstract

Much is known about the structure, function, and stability of the SecA motor ATPase that powers the secretion of periplasmic proteins across the inner membrane of Escherichia coli. Most studies of SecA are carried out in buffered sodium or potassium chloride salt solutions. However, the principal intracellular salt of E. coli is potassium glutamate (KGlu), which is known to stabilize folded proteins and protein-nucleic acid complexes. Here we report that KGlu stabilizes SecA, including its dimeric state, and increases its ATPase activity, suggesting that SecA is likely fully folded, stable, and active in vivo at 37°C. Furthermore, KGlu also stabilizes a precursor form of the secreted maltose-binding protein.

Citing Articles

Topology of the SecA ATPase Bound to Large Unilamellar Vesicles.

Roussel G, Lindner E, White S J Mol Biol. 2022; 434(12):167607.

PMID: 35489383 PMC: 10085631. DOI: 10.1016/j.jmb.2022.167607.

The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.

Roussel G, White S Biochim Biophys Acta Biomembr. 2020; 1862(9):183358.

PMID: 32416191 PMC: 7316483. DOI: 10.1016/j.bbamem.2020.183358.

Binding of SecA ATPase monomers and dimers to lipid vesicles.

Roussel G, White S Biochim Biophys Acta Biomembr. 2019; 1862(2):183112.

PMID: 31676370 PMC: 6943190. DOI: 10.1016/j.bbamem.2019.183112.

Why Nature Chose Potassium.

Danchin A, Nikel P J Mol Evol. 2019; 87(9-10):271-288.

PMID: 31659374 DOI: 10.1007/s00239-019-09915-2.

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