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, 27 June 2000
Vol. 2000, Issue 38, p. tw4
[DOI: 10.1126/stke.2000.38.tw4]

EDITORS' CHOICE

Chromatin Stimulating Phosphorylation and Acetylation

Chromatin structure plays an important role in regulating gene expression. Cheung et al. used an antibody specific for phosphorylated and acetylated histone 3 (P/A H3) to show that epidermal growth factor (EGF) stimulated the formation of this modified histone. Kinetic analysis of the phosphorylation and formation of P/A H3 suggest that acetylation occurs after phosphorylation. In support of this order of events, the yeast histone acetylase, Gcn5, showed a higher affinity for mono-phosphorylated H3 peptides in vitro. Finally, the authors used the P/A H3-specific antibody in chromatin precipitation assays to show that treatment of cells with EGF resulted in about a twofold increase in the association of the P/A H3 with the c-fos promoter. Thus, phosphorylation of histones may play a key role in identifying promoters that should be activated in response to mitogenic signals.

Cheung, P., Tanner, K.G., Cheung, W.L., Sassone-Corsi, P., Denu, J.M., and Allis, C.D. (2000) Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell 5: 905-915. [Online Journal]

Citation: Stimulating Phosphorylation and Acetylation. Sci. STKE 2000, tw4 (2000).


To Advertise     Find Products


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