| pubmed-article:9032253 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9032253 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:9032253 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:9032253 | lifeskim:mentions | umls-concept:C1337034 | lld:lifeskim |
| pubmed-article:9032253 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9032253 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9032253 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9032253 | pubmed:dateCreated | 1997-3-14 | lld:pubmed |
| pubmed-article:9032253 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9032253 | pubmed:abstractText | The gene product defective in radiosensitive CHO mutants belonging to ionizing radiation complementation group 5, which includes the extensively studied xrs mutants, has recently been identified as Ku80, a subunit of the Ku protein and a component of DNA-dependent protein kinase (DNA-PK). Several group 5 mutants, including xrs-5 and -6, lack double-stranded DNA end-binding and DNA-PK activities. In this study, we examined additional xrs mutants at the molecular and biochemical levels. All mutants examined have low or undetectable levels of Ku70 and Ku80 protein, end-binding, and DNA-PK activities. Only one mutant, xrs-6, has Ku80 transcript levels detectable by Northern hybridization, but Ku80 mRNA was detectable by reverse transcription-PCR in most other mutants. Two mutants, xrs-4 and -6, have altered Ku80 transcripts resulting from mutational changes in the genomic Ku80 sequence affecting RNA splicing, indicating that the defects in these mutants lie in the Ku80 gene rather than a gene controlling its expression. Neither of these two mutants has detectable wild-type Ku80 transcript. Since the mutation in both xrs-4 and xrs-6 cells results in severely truncated Ku80 protein, both are likely candidates to be null mutants. Azacytidine-induced revertants of xrs-4 and -6 carried both wild-type and mutant transcripts. The results with these revertants strongly support our model proposed earlier, that CHO-K1 cells carry a copy of the Ku80 gene (XRCC5) silenced by hypermethylation. Site-directed mutagenesis studies indicate that previously proposed ATP-binding and phosphorylation sites are not required for Ku80 activity, whereas N-terminal deletions of more than the first seven amino acids result in severe loss of activities. | lld:pubmed |
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| pubmed-article:9032253 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9032253 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9032253 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9032253 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9032253 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9032253 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9032253 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:LehmannA RAR | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:GelbNN | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:PriestleyAA | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:JeggoP APA | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:JacksonS PSP | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:Steingrimsdot... | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:BluntTT | lld:pubmed |
| pubmed-article:9032253 | pubmed:author | pubmed-author:SingletonB... | lld:pubmed |
| pubmed-article:9032253 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9032253 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:9032253 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9032253 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9032253 | pubmed:pagination | 1264-73 | lld:pubmed |
| pubmed-article:9032253 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:9032253 | pubmed:meshHeading | pubmed-meshheading:9032253-... | lld:pubmed |
| pubmed-article:9032253 | pubmed:meshHeading | pubmed-meshheading:9032253-... | lld:pubmed |
| pubmed-article:9032253 | pubmed:meshHeading | pubmed-meshheading:9032253-... | lld:pubmed |
