General stress response in α‐proteobacteria: PhyR and beyond
General stress response in α‐proteobacteria: PhyR and beyond
复制标题
α变形菌的一般应激反应:PhyR 及其他
DOI:
10.1111/j.1365-2958.2010.07336.x
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发表时间:
2010
影响因子:
3.6
通讯作者:
Mascher T
中科院分区:
文献类型:
--
作者:
Staroń A;Mascher T
In addition to stress‐specific responses, most bacteria can mount a general stress response (GSR), which protects the cells against a wide range of unspecific stress conditions. The best‐understood examples of GSR are the σB‐cascade ofBacillus subtilisand the RpoS response inEscherichia coli. While the latter is conserved in many other proteobacteria of the β‐, γ‐ and δ‐clades, RpoS homologues are absent in α‐proteobacteria and their GSR has long been a mystery. Recent publications finally unraveled the core of the GSR in this proteobacterial class, which is mediated by EcfG‐like σ‐factors. EcfG activity is controlled by NepR‐like anti‐σ factors and PhyR‐like proteins that act as anti‐anti‐σ factors. These unusual hybrid proteins contain an N‐terminal EcfG‐like domain that acts as a docking interface for NepR, and a C‐terminal receiver domain typical for bacterial response regulators. Upon phosphorylation, PhyR titrates NepR away from EcfG, thereby releasing the σ‐factor to recruit RNA polymerase and initiate transcription of its target genes. In this issue ofMolecular Microbiology, Herrouet al. describe the function and three‐dimensional structure of PhyR fromCaulobacter crescentus. This structure is key to understanding the mechanism of the reversible, phosphorylation‐dependent partner switching module that orchestrates the GSR in α‐proteobacteria.
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DOI:
10.1007/978-0-387-78885-2_4
发表时间:
2008-01-01
期刊:
BACTERIAL SIGNAL TRANSDUCTION: NETWORKS AND DRUG TARGETS
影响因子:
--
作者:
Hengge, Regine
通讯作者:
Hengge, Regine
影响因子:
5.4
作者:
Bourret, Robert B.
通讯作者:
Bourret, Robert B.
影响因子:
--
作者:
J. Helmann
通讯作者:
J. Helmann
影响因子:
10.5
作者:
Gao R;Stock AM
通讯作者:
Stock AM