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http://purl.uniprot.org/citations/15331764http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15331764http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15331764http://www.w3.org/2000/01/rdf-schema#comment"The structural maintenance of chromosomes (SMC) family of proteins play key roles in the organization, packaging, and repair of chromosomes. Cohesin (Smc1+3) holds replicated sister chromatids together until mitosis, condensin (Smc2+4) acts in chromosome condensation, and Smc5+6 performs currently enigmatic roles in DNA repair and chromatin structure. The SMC heterodimers must associate with non-SMC subunits to perform their functions. Using both biochemical and genetic methods, we have isolated a novel subunit of the Smc5+6 complex, Nse3. Nse3 is an essential nuclear protein that is required for normal mitotic chromosome segregation and cellular resistance to a number of genotoxic agents. Epistasis with Rhp51 (Rad51) suggests that like Smc5+6, Nse3 functions in the homologous recombination based repair of DNA damage. We previously identified two non-SMC subunits of Smc5+6 called Nse1 and Nse2. Analysis of nse1-1, nse2-1, and nse3-1 mutants demonstrates that they are crucial for meiosis. The Nse1 mutant displays meiotic DNA segregation and homologous recombination defects. Spore viability is reduced by nse2-1 and nse3-1, without affecting interhomolog recombination. Finally, genetic interactions shared by the nse mutants suggest that the Smc5+6 complex is important for replication fork stability."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e04-05-0436"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e04-05-0436"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Yates J.R. III"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Yates J.R. III"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"McDonald W.H."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"McDonald W.H."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Boddy M.N."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Boddy M.N."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Pavlova Y."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Pavlova Y."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Pebernard S."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/author"Pebernard S."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/pages"4866-4876"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/pages"4866-4876"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/title"Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3, play a crucial role in meiosis."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/title"Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3, play a crucial role in meiosis."xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/15331764http://purl.uniprot.org/core/volume"15"xsd:string