| http://purl.uniprot.org/citations/22211522 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22211522 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22211522 | http://www.w3.org/2000/01/rdf-schema#comment | "The Bacillus subtilis extracytoplasmic function (ECF) σ factor σ(M) is inducible by, and confers resistance to, several cell envelope-acting antibiotics. Here, we demonstrate that σ(M) is responsible for intrinsic β-lactam resistance, with σ(X) playing a secondary role. Activation of σ(M) upregulates several cell wall biosynthetic enzymes including one, PBP1, shown here to be a target for the beta-lactam cefuroxime. However, σ(M) still plays a major role in cefuroxime resistance even in cells lacking PBP1. To better define the role of σ(M) in β-lactam resistance, we characterized suppressor mutations that restore cefuroxime resistance to a sigM null mutant. The most frequent suppressors inactivated gdpP (yybT) which encodes a cyclic-di-AMP phosphodiesterase (PDE). Intriguingly, σ(M) is a known activator of disA encoding one of three paralogous diadenylate cyclases (DAC). Overproduction of the GdpP PDE greatly sensitized cells to β-lactam antibiotics. Conversely, genetic studies indicate that at least one DAC is required for growth with depletion leading to cell lysis. These findings support a model in which c-di-AMP is an essential signal molecule required for cell wall homeostasis. Other suppressors highlight the roles of ECF σ factors in counteracting the deleterious effects of autolysins and reactive oxygen species in β-lactam-treated cells."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-2958.2011.07953.x"xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-2958.2011.07953.x"xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/author | "Luo Y."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/author | "Luo Y."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/author | "Helmann J.D."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/author | "Helmann J.D."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/name | "Mol. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/name | "Mol. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/pages | "623-639"xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/pages | "623-639"xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/title | "Analysis of the role of Bacillus subtilis sigma(M) in beta-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/title | "Analysis of the role of Bacillus subtilis sigma(M) in beta-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis."xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/volume | "83"xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://purl.uniprot.org/core/volume | "83"xsd:string |
| http://purl.uniprot.org/citations/22211522 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22211522 |
| http://purl.uniprot.org/citations/22211522 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22211522 |
| http://purl.uniprot.org/citations/22211522 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22211522 |
| http://purl.uniprot.org/citations/22211522 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22211522 |
| http://purl.uniprot.org/uniprot/O07582 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22211522 |
| http://purl.uniprot.org/uniprot/P35165 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22211522 |