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First published online May 12, 2005

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A tale of two histone tails

In eukaryotic chromatin, histone modifications help to regulate gene expression in part by creating specific binding sites for transcriptional coactivators. For example, in response to physiological stimuli or stress, MAP-kinase-mediated phosphorylation of a subset of histone H3 molecules correlates with the induction of Fos, Jun and other immediate-early genes. Louis Mahadevan and colleagues now report that distinct pools of histone H3 are phosphorylated at either Ser10 or Ser28 by mitogen- and stress-activated kinase 1/2 (MSK1/2), which acts downstream of MAP kinases (see p. 2247). The authors use sequential immunoprecipitation and confocal immunocytochemistry to show that the two phosphoepitopes are not located on the same histone tail in vivo – both can be phosphorylated on the same tail in vitro. The authors show that limitations in the amount of kinase do not underlie the targeting of H3 phosphorylation. Instead, they suggest, targeting may be achieved through restricted availability of the histone substrate, association of the kinase with other factors, or differential phosphatase activity.

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Related articles in JCS:

MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2

Mark H. Dyson, Stuart Thomson, Masaki Inagaki, Hidemasa Goto, Simon J. Arthur, Karl Nightingale, Francisco J. Iborra, and Louis C. Mahadevan
JCS 2005 118: 2247-2259. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?