The Snf2 Homolog Fun30 Acts as a Homodimeric ATP-dependent Chromatin-remodeling Enzyme

被引：63

作者：

Awad, Salma ^{[1
,2
]}

Ryan, Daniel ^{[2
]}

Prochasson, Philippe ^{[3
]}

Owen-Hughes, Tom ^{[2
]}

Hassan, Ahmed H. ^{[1
]}

机构：

[1] United Arab Emirates Univ, Dept Biochem, Fac Med & Hlth Sci, Al Ain, U Arab Emirates

[2] Univ Dundee, Wellcome Trust Ctr Gene Regulat & Express, Sch Life Sci, Dundee DD1 5EH, Scotland

[3] Stowers Inst Med Res, Kansas City, MO 64110 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2010年 / 285卷 / 13期

基金：

英国惠康基金;

关键词：

SACCHAROMYCES-CEREVISIAE; TRANSCRIPTIONAL REGULATOR; DNA TRANSLOCATION; PROTEIN COMPLEXES; CHROMOSOME-I; HISTONE; NUCLEOSOME; BINDING; GENES; IDENTIFICATION;

D O I：

10.1074/jbc.M109.082149

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：

The Saccharomyces cerevisiae Fun30 (Function unknown now 30) protein shares homology with an extended family of Snf2-related ATPases. Here we report the purification of Fun30 principally as a homodimer with a molecular mass of about 250 kDa. Biochemical characterization of this complex reveals that it has ATPase activity stimulated by both DNA and chromatin. Consistent with this, it also binds to both DNA and chromatin. The Fun30 complex also exhibits activity in ATP-dependent chromatin remodeling assays. Interestingly, its activity in histone dimer exchange is high relative to the ability to reposition nucleosomes. Fun30 also possesses a weakly conserved CUE motif suggesting that it may interact specifically with ubiquitinylated proteins. However, in vitro Fun30 was found to have no specificity in its interaction with ubiquitinylated histones.

引用

页码：9477 / 9484

页数：8

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