| http://purl.uniprot.org/citations/18430082 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18430082 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18430082 | http://www.w3.org/2000/01/rdf-schema#comment | "Mycothiol (MSH) is a small thiol molecule with a cysteine-ligated disaccharide structure found in actinomycetes that include streptomycetes and mycobacteria. In Streptomyces coelicolor, a model organism for antibiotic production and differentiation, the amount of MSH is under the control of a sigma factor sigma(R), which is regulated by an antisigma factor RsrA with a thiol-disulphide redox switch. We found that the first gene (mshA) in the biosynthetic pathway for MSH and the gene for amidase (mca) that participates in detoxifying mycothiol-reactive drugs are under direct control of sigma(R). The sigma(R) target genes are induced not only by a thiol oxidant diamide, but also by alkylating agents that cause a rapid decrease in MSH. Expression of the sigma(R) regulon was also elevated in MSH-deficient mutants, suggesting that a decrease in the level of MSH is a natural intracellular trigger for sigma(R) activation. We found that MSH was capable of reducing RsrA to bind sigma(R), whereas glutathione was not. These results support a proposal that the RsrA-sigma(R) system senses the intracellular level of reduced MSH, and that MSH serves as a natural modulator of the transcription system for its own replenishment in addition to being a redox buffer and drug detoxifier."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-2958.2008.06191.x"xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-2958.2008.06191.x"xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/author | "Park J.H."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/author | "Park J.H."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/author | "Roe J.H."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/author | "Roe J.H."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/name | "Mol. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/name | "Mol. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/pages | "861-870"xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/pages | "861-870"xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/title | "Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/title | "Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor."xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/volume | "68"xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://purl.uniprot.org/core/volume | "68"xsd:string |
| http://purl.uniprot.org/citations/18430082 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18430082 |
| http://purl.uniprot.org/citations/18430082 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18430082 |
| http://purl.uniprot.org/citations/18430082 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18430082 |
| http://purl.uniprot.org/citations/18430082 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18430082 |
| http://purl.uniprot.org/uniprot/Q9ADA4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18430082 |
| http://purl.uniprot.org/uniprot/Q7AKG8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18430082 |