Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2002-7-8
pubmed:abstractText
In the budding yeast Saccharomyces cerevisiae, null alleles of several DNA repair and recombination genes confer defects in recombination that grow more severe with decreasing sequence length, indicating that they are required for short-sequence recombination (SSR). RAD1 and RAD10, which encode the subunits of the structure-specific endonuclease Rad1/10, are critical for SSR. MRE11, RAD50, and XRS2, which encode the subunits of M/R/X, another complex with nuclease activity, are also crucially important. Genetic evidence suggests that Rad1/10 and M/R/X act on the same class of substrates during SSR. MSH2 and MSH3, which encode subunits of Msh2/3, a complex active during mismatch repair and recombination, are also important for SSR but play a more restricted role. Additional evidence suggests that SSR is distinct from nonhomologous end joining and is superimposed upon basal homologous recombination.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10025407, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10066781, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10346816, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10357855, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10381326, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10523656, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10713167, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10801460, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10882115, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-10970737, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-11095674, http://linkedlifedata.com/resource/pubmed/commentcorrection/12101230-11259584, 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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Endonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Single-Strand Specific DNA and RNA..., http://linkedlifedata.com/resource/pubmed/chemical/DNA Repair Enzymes, http://linkedlifedata.com/resource/pubmed/chemical/RAD1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MSH2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MutS Homolog 2 Protein, http://linkedlifedata.com/resource/pubmed/chemical/RAD10 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/RAD50 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MRE11 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MSH3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/XRS2 protein, S cerevisiae
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