PHAGE SHOCK PROTEIN, A STRESS PROTEIN OF ESCHERICHIA-COLI

被引:221
作者
BRISSETTE, JL [1 ]
RUSSEL, M [1 ]
WEINER, L [1 ]
MODEL, P [1 ]
机构
[1] ROCKEFELLER UNIV, NEW YORK, NY 10021 USA
关键词
Filamentous phage; Heat shock protein; Membrane protein; Psp protein; σ[!sup]32[!/sup]-independent transcription;
D O I
10.1073/pnas.87.3.862
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Filamentous phage infection induces the synthesis of large amounts of an Escherichia coli protein, phage shock protein (Psp), the product of a previously undescribed gene. This induction is due to the phage gene IV protein, pIV, an integral membrane protein. The uninduced level of Psp is undetectable, but when induced by prolonged synthesis of pIV, it can become one of the most abundant proteins in the cell. Psp is also synthesized transiently in response to several stresses (heat, ethanol, and osmotic shock). High-level synthesis occurs only after extreme treatment. Unlike the members of the heat shock regulon, Psp induction does not require the heat shock σ factor, σ32; some stimuli that elicit σ32-dependent heat shock proteins do not induce Psp synthesis. The level of Psp induction after extreme stress is even higher in σ32 mutant cells, which are unable to mount a normal heat shock response, suggesting that these parallel stress responses are interrelated.
引用
收藏
页码:862 / 866
页数:5
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