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Identification of Residues in Chromodomain Helicase DNA-Binding Protein 1 (Chd1) Required for Coupling ATP Hydrolysis to Nucleosome Sliding.

Authors :
Patel, Ashok
McKnight, Jeffrey N.
Genzor, Pavol
Bowman, Gregory D.
Source :
Journal of Biological Chemistry. 12/23/2011, Vol. 286 Issue 51, p43984-43993. 10p.
Publication Year :
2011

Abstract

Chromatin remodelers are ATP-dependent machines responsible for directionally shifting nucleosomes along DNA. We are interested in defining which elements of the chromodomain helicase DNA-binding protein 1 (Chd1) remodeler are necessary and sufficient for sliding nucleosomes. This work focuses on the polypeptide segment that joins the ATPase motor to the C-terminal DNA-binding domain. We identify amino acid positions outside the ATPase motor that, when altered, dramatically reduce nucleosome sliding ability and yet have only ~3-fold reduction in ATPase stimulation by nucleosomes. These residues therefore appear to play a role in functionally coupling ATP hydrolysis to nucleosome sliding, and suggest that the ATPase motor requires cooperation with external elements to slide DNA past the histone core. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219258
Volume :
286
Issue :
51
Database :
Academic Search Index
Journal :
Journal of Biological Chemistry
Publication Type :
Academic Journal
Accession number :
70304541
Full Text :
https://doi.org/10.1074/jbc.M111.282970