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| pubmed-article:15527972 | lifeskim:mentions | umls-concept:C1337104 | lld:lifeskim |
| pubmed-article:15527972 | lifeskim:mentions | umls-concept:C1415549 | lld:lifeskim |
| pubmed-article:15527972 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15527972 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:15527972 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
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| pubmed-article:15527972 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:15527972 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15527972 | pubmed:dateCreated | 2004-11-5 | lld:pubmed |
| pubmed-article:15527972 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15527972 | pubmed:abstractText | We cloned cDNA encoding chicken HIRA, a homolog of Saccharomyces cerevisiae transcriptional corepressors Hir1p and Hir2p, possessing seven WD dipeptide motifs and a LXXLL motif in its N-terminal and C-terminal regions, respectively. It binds to CAF-1p48, HDAC-1 and 2, but not to CAF-1p60, p46 polypeptide and HDAC-3. The immunoprecipitation experiment involving truncated and missense mutants of HIRA and CAF-1p48 revealed not only that even one of seven WD dipeptide motifs in the N-terminal half of HIRA are necessary for the interaction with CAF-1p48, but also that those of CAF-1p48 are necessary for the interaction with HIRA. These findings indicate that the proper propeller structures of both HIRA and CAF-1p48 are necessary for their in vitro interaction. The immunoprecipitation experiment involving truncated and missense mutants of HIRA and HDAC-2 revealed that the LXXLL motif in the C-terminal half of HIRA and a C-terminal region of HDAC-2 are necessary for their in vitro interaction. Moreover, the WD dipeptide motifs and LXXLL motif of HIRA are essential for the interaction with CAF-1p48 and HDAC-2 in vivo. Taken together, these results indicate that HIRA should participate differentially in a number of DNA-utilizing processes through interactions of its distinct regions with these proteins. | lld:pubmed |
| pubmed-article:15527972 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15527972 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15527972 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15527972 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15527972 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15527972 | pubmed:issn | 0378-1119 | lld:pubmed |
| pubmed-article:15527972 | pubmed:author | pubmed-author:NakayamaTatsu... | lld:pubmed |
| pubmed-article:15527972 | pubmed:author | pubmed-author:TakamiYasunar... | lld:pubmed |
| pubmed-article:15527972 | pubmed:author | pubmed-author:AhmadAhyarA | lld:pubmed |
| pubmed-article:15527972 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15527972 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:15527972 | pubmed:volume | 342 | lld:pubmed |
| pubmed-article:15527972 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15527972 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15527972 | pubmed:pagination | 125-36 | lld:pubmed |
| pubmed-article:15527972 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15527972 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15527972 | pubmed:articleTitle | WD dipeptide motifs and LXXLL motif of chicken HIRA are essential for interactions with the p48 subunit of chromatin assembly factor-1 and histone deacetylase-2 in vitro and in vivo. | lld:pubmed |
| pubmed-article:15527972 | pubmed:affiliation | Department of Life Science, Frontier Science Research Center, Miyazaki Medical College, University of Miyazaki, 5200, Kihara, Kiyotake, Miyazaki 889-1692, Japan. | lld:pubmed |
| pubmed-article:15527972 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15527972 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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