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


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} (A.M.B.); zgdong{at} (Z.D.)

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

A Derivative of Chrysin Suppresses Two-Stage Skin Carcinogenesis by Inhibiting Mitogen- and Stress-Activated Kinase 1.
H. Liu, J. Hwang, W. Li, T. W. Choi, K. Liu, Z. Huang, J.-H. Jang, N. R. Thimmegowda, K. W. Lee, I.-J. Ryoo, et al. (2014)
Cancer Prevention Research 7, 74-85
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Nuclear CaMKII enhances histone H3 phosphorylation and remodels chromatin during cardiac hypertrophy.
S. Awad, M. Kunhi, G. H. Little, Y. Bai, W. An, D. Bers, L. Kedes, and C. Poizat (2013)
Nucleic Acids Res. 41, 7656-7672
   Abstract »    Full Text »    PDF »
Phosphorylation of Histone H2B Serine 32 Is Linked to Cell Transformation.
A. T. Y. Lau, S.-Y. Lee, Y.-M. Xu, D. Zheng, Y.-Y. Cho, F. Zhu, H.-G. Kim, S.-Q. Li, Z. Zhang, A. M. Bode, et al. (2011)
J. Biol. Chem. 286, 26628-26637
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Phosphorylation of H3S10 Blocks the Access of H3K9 by Specific Antibodies and Histone Methyltransferase: IMPLICATION IN REGULATING CHROMATIN DYNAMICS AND EPIGENETIC INHERITANCE DURING MITOSIS.
Q. Duan, H. Chen, M. Costa, and W. Dai (2008)
J. Biol. Chem. 283, 33585-33590
   Abstract »    Full Text »    PDF »
Carcinogen-induced histone alteration in normal human mammary epithelial cells.
C. Bradley, R. van der Meer, N. Roodi, H. Yan, M. B. Chandrasekharan, Z.-W. Sun, R. L. Mernaugh, and F. F. Parl (2007)
Carcinogenesis 28, 2184-2192
   Abstract »    Full Text »    PDF »
Ribosomal S6 Kinase 2 Is a Key Regulator in Tumor Promoter Induced Cell Transformation.
Y.-Y. Cho, K. Yao, H.-G. Kim, B. S. Kang, D. Zheng, A. M. Bode, and Z. Dong (2007)
Cancer Res. 67, 8104-8112
   Abstract »    Full Text »    PDF »
Yersinia YopJ Acetylates and Inhibits Kinase Activation by Blocking Phosphorylation..
S. Mukherjee, G. Keitany, Y. Li, Y. Wang, H. L. Ball, E. J. Goldsmith, and K. Orth (2006)
Science 312, 1211-1214
   Abstract »    Full Text »    PDF »

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