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The SANT domain: a unique histone-tail-binding module?

Nature Reviews Molecular Cell Biology volume 5, pages 158–163 (2004)Cite this article

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.

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Figure 1: The SANT domain is a highly conserved motif that is similar to Myb DNA-binding domains.
Figure 2: Structural modelling: the electrostatic-surface potential of selected SANT domains.
Figure 3: Combinatorial roles for distinct histone-binding modules.

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Acknowledgements

We wish to thank M. Lazar, P. Becker and C. Müller for communicating results before publication. We are particularly grateful to C. Müller for the early release of the crystal coordinates of the Iswi SANT domain, which allowed us to carry out our electrostatic analyses.

Author information

Authors and Affiliations

  1. the Whitehead Institute for Biomedical Research, Cambridge, 02142, Massachusetts, USA

    Laurie A. Boyer & Robert R. Latek

  2. part of the Program in Molecular Medicine, University of Massachusetts Medical School, Plantation Street, Worcester, 01065, Massachusetts, USA

    Craig L. Peterson

Authors
  1. Laurie A. Boyer
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  2. Robert R. Latek
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  3. Craig L. Peterson
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Corresponding author

Correspondence to Craig L. Peterson.

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Related links

Related links

DATABASES

FlyBase

ISWI

Interpro

H2A

H2B

H3

H4

Myb DBD

Swiss-Prot

BRG1

CoREST

HDAC3

HMG1

MTA2

N-CoR

SMRT

TFIIIB

Saccharomyces genome database

Ada2

Gcn5

Rsc8

Swi3

FURTHER INFORMATION

Compute pI/Mw tool

SANT supplementary information

SMART

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Boyer, L., Latek, R. & Peterson, C. The SANT domain: a unique histone-tail-binding module?. Nat Rev Mol Cell Biol 5, 158–163 (2004). https://doi.org/10.1038/nrm1314

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