General stress response in α-proteobacteria: PhyR and beyond
Publikation: Beitrag in Fachzeitschrift › Forschungsartikel › Beigetragen › Begutachtung
Beitragende
Abstract
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 σ(B)-cascade of Bacillus subtilis and the RpoS response in Escherichia coli. While the latter is conserved in many other proteobacteria of the ß-, 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 of Molecular Microbiology, Herrou et al. describe the function and three-dimensional structure of PhyR from Caulobacter crescentus. This structure is key to understanding the mechanism of the reversible, phosphorylation-dependent partner switching module that orchestrates the GSR in α-proteobacteria.
Details
Originalsprache | Englisch |
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Seiten (von - bis) | 271-277 |
Seitenumfang | 7 |
Fachzeitschrift | Molecular microbiology |
Jahrgang | 78 |
Ausgabenummer | 2 |
Publikationsstatus | Veröffentlicht - 12 Aug. 2010 |
Peer-Review-Status | Ja |
Externe IDs
Scopus | 78649371678 |
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Schlagworte
Schlagwörter
- Alphaproteobacteria/genetics, Bacterial Proteins/genetics, Gene Expression Regulation, Bacterial, Phosphorylation, Sigma Factor/genetics, Stress, Physiological