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http://purl.uniprot.org/citations/15292138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15292138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15292138http://www.w3.org/2000/01/rdf-schema#comment"In a continuing effort to identify ribonucleases that may be involved in mRNA decay in Bacillus subtilis, fractionation of a protein extract from a triple-mutant strain that was missing three previously characterized 3'-to-5' exoribonucleases (polynucleotide phosphorylase [PNPase], RNase R, and YhaM) was undertaken. These experiments revealed the presence of a high-molecular-weight nuclease encoded by the yhcR gene that was active in the presence of Ca(2+) and Mn(2+). YhcR is a sugar-nonspecific nuclease that cleaves endonucleolytically to yield nucleotide 3'-monophosphate products, similar to the well-characterized micrococcal nuclease of Staphylococcus aureus. YhcR appears to be located principally in the cell wall and is likely to be a substrate for a B. subtilis sortase. Zymogram analysis suggests that YhcR is the major Ca(2+)-activated nuclease of B. subtilis. In addition to having a unique overall domain structure, YhcR contains a hitherto unknown structural domain that we have named "NYD," for "new YhcR domain.""xsd:string
http://purl.uniprot.org/citations/15292138http://purl.org/dc/terms/identifier"doi:10.1128/jb.186.16.5376-5383.2004"xsd:string
http://purl.uniprot.org/citations/15292138http://purl.org/dc/terms/identifier"doi:10.1128/jb.186.16.5376-5383.2004"xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/author"Sanchez R."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/author"Sanchez R."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/author"Bechhofer D.H."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/author"Bechhofer D.H."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/author"Oussenko I.A."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/author"Oussenko I.A."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/pages"5376-5383"xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/pages"5376-5383"xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/title"Bacillus subtilis YhcR, a high-molecular-weight, nonspecific endonuclease with a unique domain structure."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/title"Bacillus subtilis YhcR, a high-molecular-weight, nonspecific endonuclease with a unique domain structure."xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/volume"186"xsd:string
http://purl.uniprot.org/citations/15292138http://purl.uniprot.org/core/volume"186"xsd:string
http://purl.uniprot.org/citations/15292138http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15292138
http://purl.uniprot.org/citations/15292138http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15292138
http://purl.uniprot.org/citations/15292138http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15292138
http://purl.uniprot.org/citations/15292138http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15292138