pubmed-article:10511548 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C1514559 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C0220050 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C0002085 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C1419240 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C1419243 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
pubmed-article:10511548 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
pubmed-article:10511548 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:10511548 | pubmed:dateCreated | 1999-12-6 | lld:pubmed |
pubmed-article:10511548 | 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. | lld:pubmed |
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pubmed-article:10511548 | pubmed:language | eng | lld:pubmed |
pubmed-article:10511548 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10511548 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10511548 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10511548 | pubmed:month | Oct | lld:pubmed |
pubmed-article:10511548 | pubmed:issn | 0016-6731 | lld:pubmed |
pubmed-article:10511548 | pubmed:author | pubmed-author:LivingstonD... | lld:pubmed |
pubmed-article:10511548 | pubmed:author | pubmed-author:OkagakiR JRJ | lld:pubmed |
pubmed-article:10511548 | pubmed:author | pubmed-author:AslesonE NEN | lld:pubmed |
pubmed-article:10511548 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10511548 | pubmed:volume | 153 | lld:pubmed |
pubmed-article:10511548 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10511548 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10511548 | pubmed:pagination | 681-92 | lld:pubmed |
pubmed-article:10511548 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10511548 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10511548 | 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. | lld:pubmed |
pubmed-article:10511548 | pubmed:affiliation | Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota 55455-0347, USA. | lld:pubmed |
pubmed-article:10511548 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10511548 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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