The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties

被引：28

作者：

Bonnet, Jacques ^{[1
]}

Wang, Ying-Hui ^{[2
]}

Spedale, Gianpiero ^{[3
]}

Atkinson, R. Andrew ^{[2
]}

Romier, Christophe ^{[2
]}

Hamiche, Ali ^{[1
]}

Pijnappel, W. W. M. Pim ^{[3
]}

Timmers, H. Th. Marc ^{[3
]}

Tora, Laszlo ^{[1
]}

Devys, Didier ^{[1
]}

Kieffer, Bruno ^{[2
]}

机构：

[1] Univ Strasbourg, CNRS, IGBMC, INSERM,Dept Funct Genom,UMR 7104,U964, Illkirch Graffenstaden, France

[2] Univ Strasbourg, CNRS, IGBMC, INSERM,Dept Struct Biol & Genom,UMR 7104,U964, Illkirch Graffenstaden, France

[3] Univ Med Ctr Utrecht, Dept Physiol Chem, NL-3584 CG Utrecht, Netherlands

来源：

EMBO REPORTS | 2010年 / 11卷 / 08期

关键词：

SAGA; ATXN7; ubiquitin; zinc-finger; nucleosome; MESSENGER-RNA EXPORT; SAGA COMPLEX; HISTONE H2B; DEUBIQUITINATION; TRANSCRIPTION; MODULE; DEUBIQUITYLATION; UBP8; ACTIVATION; RESTRAINTS;

D O I：

10.1038/embor.2010.98

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：612 / 618

页数：7

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