Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 10 April 2001
Vol. 2001, Issue 77, p. tw10
[DOI: 10.1126/stke.2001.77.tw10]

EDITORS' CHOICE

DNA Structure Cracking the Chromatin Code

Covalent modifications on the amino-terminal tails of the histone proteins are thought to be involved in the specification of higher-order chromatin structures that are intimately involved in processes such as gene transcription, DNA replication, and repair. For example, heterochromatin plays an important role in silencing gene expression. The protein Clr4 has been suggested to be involved in heterochromatin formation and can methylate the lysine-9 residue of the histone H3 tail. Nakayama et al. now show that Clr4-directed methylation of histone H3 corresponds with heterochromatin assembly in vivo, which is consistent with the role of Clr4 in epigenetic silencing. H3 methylation results in localization of Swi6, a homolog of the Drosophila heterochromatin protein 1. Furthermore, Clr3, a histone H3-specific deactylase, is also required for H3 methylation, Swi6 localization, and heterochromatin formation, supporting the hypothesis that a histone modification "code" exists for the establishment of chromatin structures. Berger provides an acompanying perspective.

J.-i. Nakayama, J. C. Rice, B. D. Strahl, C. D. Allis, S. I. S. Grewal, Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110-113 (2001). [Abstract] [Full Text]

S. L. Berger, The histone modification circus. Science 292, 64-65 (2001). [Full Text]

Citation: Cracking the Chromatin Code. Sci. STKE 2001, tw10 (2001).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882