期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 21, 页码 E1415-E1423出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1116887109
关键词
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资金
- National Institutes of Health [R01GM087353, R01CA093577, RR-08630]
- Department of Energy Office of Basic Energy Sciences [DE-AC02-06CH11357]
- Michigan Economic Development Corporation
- Michigan Technology Tri-Corridor [085P1000817]
alpha-Proteobacteria uniquely integrate features of two-component signal transduction (TCS) and alternative sigma factor (sigma) regulation to control transcription in response to general stress. The core of this regulatory system is the PhyR protein, which contains a sigma-like (SL) domain and a TCS receiver domain. Aspartyl phosphorylation of the PhyR receiver in response to stress signals promotes binding of the anti-sigma factor, NepR, to PhyR-SL. This mechanism, whereby NepR switches binding between its cognate s factor and phospho-PhyR (PhyR similar to P), controls transcription of the general stress regulon. We have defined the structural basis of the PhyR similar to P/NepR interaction in Caulobacter crescentus and characterized the effect of aspartyl phosphorylation on PhyR structure by molecular dynamics simulations. Our data support a model in which phosphorylation of the PhyR receiver domain promotes its dissociation from the PhyR-SL domain, which exposes the NepR binding site. A highly dynamic loop-helix region (alpha 3-alpha 4) of the PhyR-SL domain plays an important role in PhyR similar to P binding to NepR in vitro, and in stress-dependent activation of transcription in vivo. This study provides a foundation for understanding the protein-protein interactions and protein structural dynamics that underpin general stress adaptation in a large and metabolically diverse clade of the bacterial kingdom.
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