| pubmed-article:20634802 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C0678558 | lld:lifeskim |
| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:20634802 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:20634802 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:20634802 | pubmed:dateCreated | 2010-7-27 | lld:pubmed |
| pubmed-article:20634802 | pubmed:abstractText | SAGA (Spt-Ada-Gcn5 acetyltransferase), a coactivator complex involved in chromatin remodelling, harbours both histone acetylation and deubiquitination activities. ATXN7/Sgf73 and ATXN7L3, two subunits of the SAGA deubiquitination module, contain an SCA7 domain characterized by an atypical zinc-finger. We show that the yeast Sgf73-SCA7 domain is not required to recruit Sgf73 into SAGA. Instead, it binds to nucleosomes, a property that is conserved in the human ATXN7-SCA7 domain but is lost in the ATXN7L3 domain. The solution structures of the SCA7 domain of both ATXN7 and ATXN7L3 reveal a new, common zinc-finger motif at the heart of two distinct folds, providing a molecular basis for the observed functional differences. | lld:pubmed |
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| pubmed-article:20634802 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:20634802 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20634802 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20634802 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:20634802 | pubmed:issn | 1469-3178 | lld:pubmed |
| pubmed-article:20634802 | pubmed:author | pubmed-author:RomierChristo... | lld:pubmed |
| pubmed-article:20634802 | pubmed:author | pubmed-author:AtkinsonR... | lld:pubmed |
| pubmed-article:20634802 | pubmed:author | pubmed-author:TimmersH Th... | lld:pubmed |
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| pubmed-article:20634802 | pubmed:author | pubmed-author:HamicheAliA | lld:pubmed |
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| pubmed-article:20634802 | pubmed:author | pubmed-author:PijnappelW... | lld:pubmed |
| pubmed-article:20634802 | pubmed:author | pubmed-author:DevysDidierD | lld:pubmed |
| pubmed-article:20634802 | pubmed:author | pubmed-author:ToraLászlóL | lld:pubmed |
| pubmed-article:20634802 | pubmed:author | pubmed-author:WangYing-HuiY... | lld:pubmed |
| pubmed-article:20634802 | pubmed:author | pubmed-author:SpedaleGianpi... | lld:pubmed |
| pubmed-article:20634802 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20634802 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:20634802 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20634802 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20634802 | pubmed:pagination | 612-8 | lld:pubmed |
| pubmed-article:20634802 | pubmed:dateRevised | 2011-8-3 | lld:pubmed |
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| pubmed-article:20634802 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20634802 | pubmed:articleTitle | The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties. | lld:pubmed |
| pubmed-article:20634802 | pubmed:affiliation | Department of Functional Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS UMR 7104, INSERM U 964, Université de Strasbourg, Illkirch, France. | lld:pubmed |
| pubmed-article:20634802 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20634802 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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