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http://purl.uniprot.org/citations/9236119http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9236119http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9236119http://www.w3.org/2000/01/rdf-schema#comment"Endonuclease I is a DNA junction-selective resolving enzyme from bacteriophage T7. Using a nuclease-defective mutant that retains normal binding to DNA we show that the protein binds to four-way DNA junctions as a dimer, in common with other junction-resolving enzymes studied. Gel filtration and chemical crosslinking indicate that endonuclease I also exists in free solution as a dimer together with a tetramer and higher molecular mass aggregates. However, in marked contrast with other junction-resolving enzymes, there is no detectable subunit exchange under normal conditions. Only by exposure to 6 M urea could we induce subunit exchange, and this was used to generate heterodimeric species containing one active and one inactive subunit. Using a supercoil-stabilised cruciform substrate we demonstrate that an active subunit of endonuclease I can act as a junction-specific nuclease in a heterodimeric combination with an inactive subunit. However, the two subunits of a fully active homodimeric enzyme each cleave the phosphodiester backbone of a cruciform within the lifetime of the DNA-protein complex."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1997.1128"xsd:string
http://purl.uniprot.org/citations/9236119http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1997.1128"xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/author"Lilley D.M."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/author"Lilley D.M."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/author"Parkinson M.J."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/author"Parkinson M.J."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/pages"169-178"xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/pages"169-178"xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/title"The junction-resolving enzyme T7 endonuclease I: quaternary structure and interaction with DNA."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/title"The junction-resolving enzyme T7 endonuclease I: quaternary structure and interaction with DNA."xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/9236119http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/9236119http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9236119
http://purl.uniprot.org/citations/9236119http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9236119
http://purl.uniprot.org/citations/9236119http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9236119
http://purl.uniprot.org/citations/9236119http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9236119
http://purl.uniprot.org/uniprot/P00641http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9236119
http://purl.uniprot.org/uniprot/P00641#attribution-4EE43E809AB57B70D96B7140B4C272D0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9236119