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Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR
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Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR
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Journal Article
Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR
2013
Overview
Quinone molecules are intracellular electron-transport carriers, as well as critical intra- and extracellular signals. However, transcriptional regulation of quinone signaling and its molecular basis are poorly understood. Here, we identify a thiol-stress-sensing regulator YodB family transcriptional regulator as a central component of quinone stress response of Staphylococcus aureus , which we have termed the quinone-sensing and response repressor (QsrR). We also identify and confirm an unprecedented quinone-sensing mechanism based on the S-quinonization of the essential residue Cys-5. Structural characterizations of the QsrR–DNA and QsrR–menadione complexes further reveal that the covalent association of menadione directly leads to the release of QsrR from operator DNA following a 10° rigid-body rotation as well as a 9-Å elongation between the dimeric subunits. The molecular level characterization of this quinone-sensing transcriptional regulator provides critical insights into quinone-mediated gene regulation in human pathogens.
Publisher
National Academy of Sciences,National Acad Sciences,National Academy of Sciences, Washington, DC (United States)
Subject
Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Dimers
/ DNA
/ Gene Expression Regulation, Bacterial - physiology
/ Genes
/ Humans
/ Protein Processing, Post-Translational - physiology
/ Protein Structure, Quaternary
/ Quinones
/ Repressor Proteins - chemistry
/ Repressor Proteins - genetics
/ Repressor Proteins - metabolism
/ Signal Transduction - physiology
/ Staphylococcus aureus - chemistry
/ Staphylococcus aureus - genetics
