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http://purl.uniprot.org/citations/22578863http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22578863http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22578863http://www.w3.org/2000/01/rdf-schema#comment"GTP-binding proteins (G-proteins) are highly conserved signaling molecules that participate in cellular signaling and bacterial pathogenesis by regulating the activity of cognate GTPases. However, the exact role of G-proteins in the pathogenesis of Mycobacterium tuberculosis is poorly understood. The complete genome sequence of M. tuberculosis H(37)Rv, suggests the presence of several homologs of bacterial G-proteins. In the present study, three G-proteins, Era, Obg and LepA of M. tuberculosis H(37)Rv were cloned and expressed in Escherichia coli. Purified proteins showed GTP-binding and hydrolyzing activities. A point mutation in the conserved GTP-binding motif, AspXXGly (Asp to Ala) in Era (Asp-258) and Obg (Asp-212) proteins resulted in the loss of the associated activities, confirming that known key residues in well-established G-proteins are also conserved in mycobacterial homologs. This study confirms that Era, Obg and LepA of M. tuberculosis H(37)Rv possess GTPase activity and provide a platform to understand the physiological significance of these proteins in associated pathogenesis."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.org/dc/terms/identifier"doi:10.1016/j.enzmictec.2007.08.008"xsd:string
http://purl.uniprot.org/citations/22578863http://purl.org/dc/terms/identifier"doi:10.1016/j.enzmictec.2007.08.008"xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Singh Y."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Singh Y."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Chopra P."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Chopra P."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Bedwal R.S."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Bedwal R.S."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Meena L.S."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/author"Meena L.S."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/name"Enzyme Microb. Technol."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/name"Enzyme Microb. Technol."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/pages"138-144"xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/pages"138-144"xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/title"Cloning and characterization of GTP-binding proteins of Mycobacterium tuberculosis H37Rv."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/title"Cloning and characterization of GTP-binding proteins of Mycobacterium tuberculosis H37Rv."xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/22578863http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/22578863http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22578863
http://purl.uniprot.org/citations/22578863http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22578863