Diverse regulation of SNF2h chromatin remodeling by noncatalytic subunits.
SNF2h-based ATP-dependent chromatin remodeling complexes diverge in composition, nuclear localization, and biological function. Such differences have led to the hypothesis that SNF2h complexes differ mechanistically. One proposal is that the complexes have different functional interactions with the naked DNA adjacent to the nucleosome. We have used a series of templates with defined nucleosomal position and differing amounts and placement of adjacent DNA to compare the relative activities of SNF2h and SNF2h complexes. The complexes hACF, CHRAC, WICH, and RSF all displayed differences in functional interactions with these templates, which we attribute to the differences in the noncatalytic subunit. We suggest that the ability to sense adjacent DNA is a general property of the binding partners of SNF2h and that each partner provides distinct regulation that contributes to distinct cellular function.
Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
Xi
X
He
Hua-Ying
HY
Fan
Joseph D
JD
Garlick
Robert E
RE
Kingston
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D020134:Catalytic Domain; D042002:Chromatin Assembly and Disassembly; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D046912:Multiprotein Complexes / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism; D011485:Protein Binding; D013698:Templates, Genetic
D002868:Chromosomal Proteins, Non-Histone; D046912:Multiprotein Complexes; D009707:Nucleosomes; D004247:DNA; D000251:Adenosine Triphosphatases; C409462:SMARCA5 protein, human