RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/10681538http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10681538http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10681538http://www.w3.org/2000/01/rdf-schema#comment"The formation of triple helical DNA has been evoked in several cellular processes including transcription, replication, and recombination. Using conventional and affinity chromatography, we purified from Saccharomyces cerevisiae whole-cell extract a 35-kDa protein that avidly and specifically bound a purine motif triplex (with a K(d) of 61 pM) but not a pyrimidine motif triplex or duplex DNA. Peptide microsequencing identified this protein as the product of the STM1 gene. Confirmation that Stm1p is a purine motif triplex-binding protein was obtained by electrophoretic mobility shift assays using either bacterially expressed, recombinant Stm1p or whole-cell extracts from stm1Delta yeast. Stm1p has previously been identified as G4p2, a G-quartet nucleic acid-binding protein. This suggests that some proteins actually recognize features shared by G4 DNA and purine motif triplexes, e.g. Hoogsteen hydrogen-bonded guanines. Genetically, the STM1 gene has been identified as a multicopy suppressor of mutations in several genes involved in mitosis (e.g. TOM1, MPT5, and POP2). A possible role for multiplex DNA and its binding proteins in mitosis is discussed."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.8.5573"xsd:string
http://purl.uniprot.org/citations/10681538http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.8.5573"xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/author"Van Dyke M.W."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/author"Van Dyke M.W."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/author"Musso M."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/author"Musso M."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/author"Nelson L.D."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/author"Nelson L.D."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/pages"5573-5581"xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/pages"5573-5581"xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/title"The yeast STM1 gene encodes a purine motif triple helical DNA-binding protein."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/title"The yeast STM1 gene encodes a purine motif triple helical DNA-binding protein."xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10681538http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10681538http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10681538
http://purl.uniprot.org/citations/10681538http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10681538
http://purl.uniprot.org/citations/10681538http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10681538
http://purl.uniprot.org/citations/10681538http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10681538