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http://purl.uniprot.org/citations/14762009http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14762009http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14762009http://www.w3.org/2000/01/rdf-schema#comment"Bacillus subtilis contains seven extracytoplasmic-function sigma factors that activate partially overlapping regulons. We here identify four additional members of the sigma(X) regulon, pbpX (penicillin-binding protein), ywnJ, the dlt operon (D-alanylation of teichoic acids), and the pss ybfM psd operon (phosphatidylethanolamine biosynthesis). Modification of teichoic acids by esterification with D-alanine and incorporation of phosphatidylethanolamine into the cell membrane have a common consequence: in both cases positively charged amino groups are introduced into the cell envelope. The resulting reduction in the net negative charge of the cell envelope has been previously implicated as a resistance mechanism specific for cationic antimicrobial peptides. Consistent with this notion, we find that both sigX and dltA mutants are more sensitive to nisin than wild-type cells. We conclude that activation of the sigma(X) regulon serves to alter cell surface properties to provide protection against antimicrobial peptides."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.org/dc/terms/identifier"doi:10.1128/jb.186.4.1136-1146.2004"xsd:string
http://purl.uniprot.org/citations/14762009http://purl.org/dc/terms/identifier"doi:10.1128/jb.186.4.1136-1146.2004"xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/author"Cao M."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/author"Cao M."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/author"Helmann J.D."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/author"Helmann J.D."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/pages"1136-1146"xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/pages"1136-1146"xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/title"The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/title"The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides."xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/volume"186"xsd:string
http://purl.uniprot.org/citations/14762009http://purl.uniprot.org/core/volume"186"xsd:string
http://purl.uniprot.org/citations/14762009http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14762009
http://purl.uniprot.org/citations/14762009http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14762009
http://purl.uniprot.org/citations/14762009http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14762009
http://purl.uniprot.org/citations/14762009http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14762009
http://purl.uniprot.org/uniprot/O31773http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/14762009
http://purl.uniprot.org/uniprot/O31773#attribution-FDF55E5C115060DDA0369CA95B22C0D0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/14762009