In vivo localizations of membrane stress controllers PspA and PspG in Escherichia coli

被引:53
作者
Engl, Christoph [1 ]
Jovanovic, Goran [1 ]
Lloyd, Louise J. [1 ]
Murray, Heath [4 ]
Spitaler, Martin [2 ]
Ying, Liming [3 ]
Errington, Jeff [4 ]
Buck, Martin [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Biol, London SW7 2AZ, England
[2] Univ London Imperial Coll Sci Technol & Med, FILM, London SW7 2AZ, England
[3] Univ London Imperial Coll Sci Technol & Med, Natl Heart & Lung Inst, London SW7 2AZ, England
[4] Univ Newcastle, Inst Cell & Mol Biosci, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England
基金
英国生物技术与生命科学研究理事会;
关键词
PHAGE-SHOCK-PROTEIN; YERSINIA-ENTEROCOLITICA; GENE-EXPRESSION; CELL-SHAPE; ACTIN HOMOLOG; III SECRETION; Z-RING; IDENTIFICATION; SYSTEM; MREB;
D O I
10.1111/j.1365-2958.2009.06776.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The phage shock protein (Psp) response in Gram-negative bacteria counteracts membrane stress. Transcription of the PspF regulon (pspABCDE and pspG) in Escherichia coli is induced upon stresses that dissipate the proton motive force (pmf). Using GFP fusions we have visualized the subcellular localizations of PspA (a negative regulator and effector of Psp) and PspG (an effector of Psp). It has previously been proposed that PspA evenly coates the inner membrane of the cell. We now demonstrate that instead of uniformly covering the entire cell, PspA (and PspG) is highly organized into what appear to be distinct functional classes (complexes at the cell pole and the lateral cell wall). Real-time observations revealed lateral PspA and PspG complexes are highly mobile, but absent in cells lacking MreB. Without the MreB cytoskeleton, induction of the Psp response is still observed, yet these cells fail to maintain pmf under stress conditions. The two spatial subspecies therefore appear to be dynamically and functionally distinct with the polar clusters being associated with sensory function and the mobile complexes with maintenance of pmf.
引用
收藏
页码:382 / 396
页数:15
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