Review
Nature Reviews Molecular Cell Biology 8, 983-994 (December 2007) | doi:10.1038/nrm2298
Multivalent engagement of chromatin modifications by linked binding modules
Alexander J. Ruthenburg1, Haitao Li2, Dinshaw J. Patel2 & C. David Allis1 About the authors
Abstract
Various chemical modifications on histones and regions of associated DNA play crucial roles in genome management by binding specific factors that, in turn, serve to alter the structural properties of chromatin. These so-called effector proteins have typically been studied with the biochemist's paring knife — the capacity to recognize specific chromatin modifications has been mapped to an increasing number of domains that frequently appear in the nuclear subset of the proteome, often present in large, multisubunit complexes that bristle with modification-dependent binding potential. We propose that multivalent interactions on a single histone tail and beyond may have a significant, if not dominant, role in chromatin transactions.
- View At a Glance
Author affiliations
- Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10065, USA.
- Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Correspondence to: C. David Allis1 Email: alliscd@rockefeller.edu
Correspondence to: Dinshaw J. Patel2 Email: pateld@mskcc.org
Correspondence to: Alexander J. Ruthenburg1 Email: aruthenbur@rockefeller.edu
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
It takes a PHD to interpret histone methylationNature Structural & Molecular Biology News and Views (01 Jul 2006)
Trans-tail histone modifications: wedge or bridge?Nature Structural Biology News and Views (01 Aug 2002)
See all 3 matches for News And ViewsRESEARCH
Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURFNature Letters to Editor (06 Jul 2006)
See all 2 matches for Research