Perspectives
Nature Reviews Molecular Cell Biology 5, 158-163 (February 2004) | doi:10.1038/nrm1314
Opinion: The SANT domain: a unique histone-tail-binding module?
Laurie A. Boyer1, Robert R. Latek1 & Craig L. Peterson2 About the authors
Abstract
Chromatin-remodelling complexes have an important role in all DNA-mediated processes and, although much is known about how these enzymes regulate chromosomal DNA accessibility, how they interact with their histone substrates has remained unclear. However, recent studies have indicated that the SANT domain has a central role in chromatin remodelling by functioning as a unique histone-interaction module that couples histone binding to enzyme catalysis.
Author affiliations
- Laurie A. Boyer and Robert R. Lateck are at the Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142, USA.
- Craig L. Peterson is part of the Program in Molecular Medicine, University of Massachusetts Medical School, Plantation Street, Worcester, Massachusetts 01065, USA.
Correspondence to: Craig L. Peterson2 Email: craig.peterson@umassmed.edu
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