Purification and characterization of a human factor that assembles and remodels chromatin

被引:131
作者
LeRoy, G
Loyola, A
Lane, WS
Reinberg, D [1 ]
机构
[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Div Nucle Acid Enzymol,Howard Hughes Med Inst, Piscataway, NJ 08854 USA
[2] Harvard Univ, Harvard Microchem Facil, Cambridge, MA 02138 USA
关键词
D O I
10.1074/jbc.C000093200
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
We have previously reported the isolation and characterization of a nucleosome remodeling and spacing factor, RSF. One of the RSF subunits is hSNF2h, a SNF2 homologue. Here we set out to isolate and characterize other hSNF2h-containing complexes. We have identified a novel hSNF2h complex that facilitates ATP-dependent chromatin assembly with the histone chaperone NAP-1. The complex possesses ATPase activity that is DNA-dependent and nucleosome-stimulated. This complex is capable of facilitating ATP-dependent nucleosome remodeling and transcription initiation from chromatin templates. In addition to hSNF2h, this complex also contains a 190-kDa protein encoded by the BAZ1A gene. Since both subunits are homologues of the Drosophila ACF complex (ATP-utilizing chromatin assembly and remodeling factor), we have named this factor human ACF or hACF.
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页码:14787 / 14790
页数:4
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