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Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica
被引:30
作者:
Horstman, N. Kaye
[1
]
Darwin, Andrew J.
[1
]
机构:
[1] NYU, Sch Med, Dept Microbiol, New York, NY 10016 USA
关键词:
SECRETIN-INDUCED STRESS;
PROTON MOTIVE FORCE;
ESCHERICHIA-COLI;
GENE-EXPRESSION;
PSP RESPONSE;
SYSTEM;
IDENTIFICATION;
CONSTRUCTION;
VIRULENCE;
CLONING;
D O I:
10.1111/j.1365-2958.2012.08120.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 bacterial phage shock protein (Psp) stress response system is activated by events affecting the cytoplasmic membrane. In response, Psp protein levels increase, including PspA, which has been implicated as the master effector of stress tolerance. Yersinia enterocolitica and related bacteria with a defective Psp system are highly sensitive to the mislocalization of pore-forming secretin proteins. However, why secretins are toxic to psp null strains, whereas some other Psp inducers are not, has not been explained. Furthermore, previous work has led to the confounding and disputable suggestion that PspA is not involved in mitigating secretin toxicity. Here we have established a correlation between the amount of secretin toxicity in a psp null strain and the extent of cytoplasmic membrane permeability to large molecules. This leads to a morphological change resembling cells undergoing plasmolysis. Furthermore, using novel strains with dis-regulated Psp proteins has allowed us to obtain unequivocal evidence that PspA is not required for secretin-stress tolerance. Together, our data suggest that the mechanism by which secretin multimers kill psp null cells is by causing a profound defect in the cytoplasmic membrane permeability barrier. This allows lethal molecular exchange with the environment, which the PspB and PspC proteins can prevent.
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页码:445 / 460
页数:16
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