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http://purl.uniprot.org/citations/12940997http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12940997http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12940997http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/12940997http://www.w3.org/2000/01/rdf-schema#comment"SpoIVB is the critical determinant for intercompartmental signalling of pro-sigmaK processing during sporulation in Bacillus subtilis. We show here that the SpoIVB serine peptidase can cleave the SpoIVFA protein, which is one component of the pro-sigmaK processing complex. SpoIVFA has been shown elsewhere (Rudner, D.Z., and Losick, R., 2002, Genes Dev 16: 1007-1018) to tether BofA and SpoIVFB in a membrane-embedded heteroligomeric complex in which BofA directly inhibits the activity of SpoIVFB. Cleavage of SpoIVFA would provide the necessary signal to dissolve this complex and release BofA-mediated inhibition on the zinc metalloprotease, SpoIVFB, that is responsible for cleaving pro-sigmaK to its mature form. We also show that the SpoIVB PDZ domain is required for self-recognition and trans cleavage of SpoIVB and is probably also used to target an internal motif within the C-terminal region of SpoIVFA exposed in the space between the inner and outer forespore membranes. This work reveals the mechanism of intercompartmental signalling and provides a unified model as to how sigmaK-directed gene expression in the mother cell is co-ordinated with events in the forespore chamber."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-2958.2003.03651.x"xsd:string
http://purl.uniprot.org/citations/12940997http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-2958.2003.03651.x"xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/author"Cutting S.M."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/author"Cutting S.M."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/author"Dong T.C."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/author"Dong T.C."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/pages"1425-1434"xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/pages"1425-1434"xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/title"SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of Pro-sigmaK in Bacillus subtilis."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/title"SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of Pro-sigmaK in Bacillus subtilis."xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/volume"49"xsd:string
http://purl.uniprot.org/citations/12940997http://purl.uniprot.org/core/volume"49"xsd:string
http://purl.uniprot.org/citations/12940997http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12940997
http://purl.uniprot.org/citations/12940997http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12940997
http://purl.uniprot.org/citations/12940997http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12940997
http://purl.uniprot.org/citations/12940997http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12940997
http://purl.uniprot.org/citations/12940997http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12940997