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rdf:type |
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lifeskim:mentions |
umls-concept:C0002085,
umls-concept:C0043393,
umls-concept:C0220050,
umls-concept:C0301625,
umls-concept:C0332281,
umls-concept:C0441655,
umls-concept:C0444669,
umls-concept:C1419240,
umls-concept:C1419243,
umls-concept:C1514559,
umls-concept:C1706395,
umls-concept:C1707271
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pubmed:issue |
2
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pubmed:dateCreated |
1999-12-6
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pubmed:abstractText |
C-terminal rad52 truncation and internal deletion mutants were characterized for their ability to repair MMS-induced double-strand breaks and to produce viable spores during meiosis. The rad52-Delta251 allele, encoding the N-terminal 251 amino acids of the predicted 504-amino-acid polypeptide, supports partial activity for both functions. Furthermore, RAD51 overexpression completely suppresses the MMS sensitivity of a rad52-Delta251 mutant. The absence of the C terminus in the truncated protein makes it likely that suppression occurs by bypassing the C-terminal functions of Rad52p. RAD51 overexpression does not suppress the low level of spore viability that the rad52-Delta251 allele causes and only partially suppresses the defect in rad52 alleles encoding the N-terminal 292 or 327 amino acids. The results of this study also show that intragenic complementation between rad52 alleles is governed by a complex relationship that depends heavily on the two alleles involved and their relative dosage. In heteroallelic rad52 diploids, the rad52-Delta251 allele does not complement rad52 missense mutations altering residues 61 or 64 in the N terminus. However, complementation is achieved with each of these missense alleles when the rad52-Delta251 allele is overexpressed. Complementation also occurs between rad52-Delta327 and an internal deletion allele missing residues 210 through 327. We suggest that the first 251 amino acids of Rad52p constitute a core domain that provides critical RAD52 activities.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-10200253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-10227297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-1316273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-1544568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-195865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-2005894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-3043193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-388424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-7635279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-7862153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-7982574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-8370524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-8387915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-8417987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-8595665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-8769646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-8855248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-8879274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9294257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9353267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9450758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9450759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9450760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9619627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9632824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10511548-9837724
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0016-6731
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
153
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
681-92
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10511548-Alleles,
pubmed-meshheading:10511548-Crosses, Genetic,
pubmed-meshheading:10511548-DNA-Binding Proteins,
pubmed-meshheading:10511548-Diploidy,
pubmed-meshheading:10511548-Fungal Proteins,
pubmed-meshheading:10511548-Gene Expression Regulation, Fungal,
pubmed-meshheading:10511548-Genotype,
pubmed-meshheading:10511548-Haploidy,
pubmed-meshheading:10511548-Methyl Methanesulfonate,
pubmed-meshheading:10511548-Mutagenesis,
pubmed-meshheading:10511548-Rad51 Recombinase,
pubmed-meshheading:10511548-Rad52 DNA Repair and Recombination Protein,
pubmed-meshheading:10511548-Saccharomyces cerevisiae,
pubmed-meshheading:10511548-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10511548-Sequence Deletion,
pubmed-meshheading:10511548-Spores, Fungal,
pubmed-meshheading:10511548-Suppression, Genetic
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pubmed:year |
1999
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pubmed:articleTitle |
A core activity associated with the N terminus of the yeast RAD52 protein is revealed by RAD51 overexpression suppression of C-terminal rad52 truncation alleles.
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pubmed:affiliation |
Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota 55455-0347, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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