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.

Subscribe

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.

Abstract: The physiological state of a eukaryotic cell is determined by endogenous and exogenous signals, and often the endpoint of the pathways that transmit these signals is DNA. DNA is organized into chromatin, a nucleoprotein complex, which not only facilitates the packaging of DNA within the nucleus but also serves as an important factor in the regulation of gene function. The nucleosome is the basic unit of chromatin and generally consists of approximately two turns of DNA wrapped around an octamer of core histone proteins. Each histone also contains an accessible N-terminal tail that extends outside the chromatin complex and is subject to posttranslational modifications that are crucial in the regulation of gene expression. Two distinct categories of histone posttranslational modification have been observed: (i) inducible or stimulation-dependent and (ii) mitosis-dependent. Stimulation by mitogens or stress leads to rapid transient posttranslational modifications of histones, in particular histone H3, which are mechanistically and temporarily distinct from modifications associated with mitosis. This Review focuses mainly on the inducible phosphorylation of histone H3 brought about by different stimuli, such as epidermal growth factor, 12-O-tetradecanoylphorbol-13-acetate, arsenite, or ultraviolet radiation. We examine the most recent, and at times controversial, research data concerning the identity of the histone H3 kinases responsible for this phosphorylation. In addition, the interdependence of phosphorylation and acetylation will be discussed in light of data showing patterns of inducible modification at specific genes.

*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).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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 »

To Advertise     Find Products


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