Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.
Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two alpha-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate.
Grüne
Tim
T
European Molecular Biology Laboratory, Grenoble Outstation, B.P. 181, F 38042 Grenoble 9, France.
Brzeski
Jan
J
Eberharter
Anton
A
Clapier
Cedric R
CR
Corona
Davide F V
DF
Becker
Peter B
PB
Müller
Christoph W
CW
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002843:Chromatin / Q000378:metabolism; D018360:Crystallography, X-Ray; D004331:Drosophila melanogaster / Q000378:metabolism; D017353:Gene Deletion; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D020598:Proto-Oncogene Proteins c-myb / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013997:Time Factors; D014157:Transcription Factors / Q000378:metabolism*
D002843:Chromatin; C086468:ISWI protein; D009707:Nucleosomes; D020598:Proto-Oncogene Proteins c-myb; D014157:Transcription Factors; D000251:Adenosine Triphosphatases