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http://purl.uniprot.org/citations/11172710http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11172710http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11172710http://www.w3.org/2000/01/rdf-schema#comment"Polymerase gamma, which replicates and repairs mitochondrial DNA, requires the Pol gamma B subunit for processivity. We determined the crystal structure of mouse Pol gamma B, a core component of the mitochondrial replication machinery. Pol gamma B shows high similarity to glycyl-tRNA synthetase and dimerizes through an unusual intermolecular four-helix bundle. A human Pol gamma B mutant lacking the four-helix bundle failed to dimerize in solution or to stimulate the catalytic subunit Pol gamma A, but retained the ability to bind with Pol gamma A to a primer-template construct, indicating that the functional holoenzyme contains two Pol gamma B molecules. Other mutants retained stimulatory activity but lost the ability to bind folded ssDNA. These results suggest that the Pol gamma B dimer contains distinct sites for Pol gamma A binding, dimerization, and DNA binding."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(01)00153-8"xsd:string
http://purl.uniprot.org/citations/11172710http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(01)00153-8"xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Kisker C."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Kisker C."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Theis K."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Theis K."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Bogenhagen D.F."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Bogenhagen D.F."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Carrodeguas J.A."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/author"Carrodeguas J.A."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/pages"43-54"xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/pages"43-54"xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/title"Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/title"Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer."xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/11172710http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/11172710http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11172710
http://purl.uniprot.org/citations/11172710http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11172710