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Sci. STKE, 26 April 2005
Vol. 2005, Issue 281, p. re4
[DOI: 10.1126/stke.2812005re4]

REVIEWS

Inducible Covalent Posttranslational Modification of Histone H3

Ann M. Bode* and Zigang Dong*

Hormel Institute, University of Minnesota, 801 16th Ave NE, Austin, MN 55912, USA.

Gloss: The cellular response to stress is determined by intracellular communication systems that end in the initiation of gene expression, which is tailored to fit the needs of the individual cell. DNA is organized into chromatin, which facilitates the packaging of DNA within the nucleus and also is extremely important in the regulation of gene function. The nucleosome is the basic unit of chromatin and consists of about two turns of DNA wrapped around eight core histone proteins. Each histone protein has an accessible N-terminal tail that extends outside the complex, and this tail is subject to modifications needed in the regulation of gene expression. Histone modifications can be induced by specific stimuli or are associated with mitosis. Stimulation by stress leads to rapid short-lived modifications of histones, in particular histone H3, which are different from modifications associated with mitosis. This STKE Review, with two figures, two tables, and 149 citations, focuses mainly on the inducible phosphorylation of histone H3 brought about by different stimuli and examines the most recent research data concerning the identity of the histone H3 kinases responsible for this phosphorylation.

*Corresponding authors. Telephone, 507-437-9600; fax, 507-437-9606; e-mail, ambode{at}hi.umn.edu (A.M.B.); zgdong{at}hi.umn.edu (Z.D.)

Citation: A. M. Bode, Z. Dong, Inducible Covalent Posttranslational Modification of Histone H3. Sci. STKE 2005, re4 (2005).

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