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Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.
- Source :
-
Molecular cell [Mol Cell] 2003 Aug; Vol. 12 (2), pp. 449-60. - Publication Year :
- 2003
-
Abstract
- 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.
- Subjects :
- Adenosine Triphosphatases chemistry
Amino Acid Sequence
Animals
Binding Sites
Chromatin metabolism
Crystallography, X-Ray
Drosophila melanogaster metabolism
Gene Deletion
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Proto-Oncogene Proteins c-myb metabolism
Sequence Homology, Amino Acid
Time Factors
Adenosine Triphosphatases metabolism
Nucleosomes metabolism
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 12
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 14536084
- Full Text :
- https://doi.org/10.1016/s1097-2765(03)00273-9