ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural basis of a protein partner switch that regulates the general stress response of α-proteobacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 50 citations in OpenAlex.
- Review
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.The Journal of biological chemistry · 2025Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.bioRxiv : the preprint server for biology · 2025Article
- The functional differences between paralogous regulators define the control of the general stress response in Sphingopyxis granuli TFA.Environmental microbiology · 2022Article
- Transcriptional regulation by σ factor phosphorylation in bacteria.Nature microbiology · 2020Article
- Structural basis for transcription activation by Crl through tethering of σProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Complex general stress response regulation in Sphingomonas melonis Fr1 revealed by transcriptional analyses.Scientific reports · 2019Article
- Structural basis for inhibition of a response regulator of σGenes & development · 2019Article
- Diversity, versatility and complexity of bacterial gene regulation mechanisms: opportunities and drawbacks for applications in synthetic biology.FEMS microbiology reviews · 2019Review
- The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor.Nucleic acids research · 2018Article
- Bacterial sensing: A putative amphipathic helix in RsiV is the switch for activating σV in response to lysozyme.PLoS genetics · 2018Article
- Allosteric control of a bacterial stress response system by an anti-σ factor.Molecular microbiology · 2018Article
- Themes and variations in gene regulation by extracytoplasmic function (ECF) sigma factors.Current opinion in microbiology · 2017Review
- Local and global regulation of transcription initiation in bacteria.Nature reviews. Microbiology · 2016Review
- Brucella abortus ΔrpoE1 confers protective immunity against wild type challenge in a mouse model of brucellosis.Vaccine · 2016Article
- Basis of Mutual Domain Inhibition in a Bacterial Response Regulator.Cell chemical biology · 2016Article
- Transcriptomic analysis of the stationary phase response regulator SpdR in Caulobacter crescentus.BMC microbiology · 2016Article
- Multiple σEcfG and NepR Proteins Are Involved in the General Stress Response in Methylobacterium extorquens.PloS one · 2016Article
- Streptococcus mutans copes with heat stress by multiple transcriptional regulons modulating virulence and energy metabolism.Scientific reports · 2015Article
- Structured and Dynamic Disordered Domains Regulate the Activity of a Multifunctional Anti-σ Factor.mBio · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
α-Proteobacteria uniquely integrate features of two-component signal transduction (TCS) and alternative sigma factor (σ) regulation to control transcription in response to general stress. The core of this regulatory system is the PhyR protein, which contains a σ-like (SL) domain and a TCS receiver domain. Aspartyl phosphorylation of the PhyR receiver in response to stress signals promotes binding of the anti-σ factor, NepR, to PhyR-SL. This mechanism, whereby NepR switches binding between its cognate σ factor and phospho-PhyR (PhyR∼P), controls transcription of the general stress regulon. We have defined the structural basis of the PhyR∼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 (α3-α4) of the PhyR-SL domain plays an important role in PhyR∼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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