Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-7-27
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-10212987, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-11395415, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-12516863, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-12522306, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-14563679, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-14630937, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-14660634, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-14718168, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-15115762, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-15260971, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-15282323, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-15657441, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-15657442, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-15772752, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-15822098, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-17380162, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-17694076, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-17694077, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-18206972, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-18206973, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-18488019, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-18603431, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-20395473, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-20434206, http://linkedlifedata.com/resource/pubmed/commentcorrection/20634802-9305837
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1469-3178
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
612-8
pubmed:dateRevised
2011-8-3
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties.
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.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't