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Activating mutations in quorum-sensing regulator Rgg2 and its conformational flexibility in the absence of an intermolecular disulfide bond
Rap/Rgg/NprR/PlcR/PrgX (RRNPP) quorum-sensing systems use extracellular peptide pheromones that are detected by cytoplasmic receptors to regulate gene expression in firmicute bacteria. Rgg-type receptors are allosterically regulated through direct pheromone binding to control transcriptional activit...
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| Foilsithe in: | J Biol Chem |
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| Main Authors: | , , , , , |
| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
American Society for Biochemistry and Molecular Biology
2017
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5733591/ https://ncbi.nlm.nih.gov/pubmed/29030429 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M117.801670 |
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