Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns

Stefan Winter, Wolfgang Fischle and Christian Seiser

volume 7 | issue 10

15 May 2008
Pages: 1336 - 1342

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Post-translational modifications of histones are determining factors in the global and local regulation of genome activity. Phosphorylation of histone H3 is globally associated with mitotic chromatin compaction but occurs in a much more restricted manner during interphase transcriptional regulation of a limited subset of genes. In the course of gene regulation, serine 10 phosphorylation at histone H3 is targeted to a very small fraction of nucleosomes that is highly susceptible to additional acetylation events. Recently, we and others have identified 14-3-3 as a binding protein that recognizes both phosphorylated serine 10 and phosphorylated serine 28 on histone H3. In vitro, the affinity of 14-3-3 for phosphoserine 10 is weak but becomes significantly increased by additional acetylation of either lysine 9 or lysine 14 on the same histone tail. In contrast, the histone H3S28 site matches elements of 14-3-3 high affinity consensus motifs. This region mediates an initial stronger interaction that is less susceptible to modulation by “auxiliary” modifications. Here we discuss the binding of 14-3-3 proteins to histone H3 in detail and putative biological implications of these interactions.

Authors

Stefan Winter

Medical University of Vienna; Vienna, Austria

Wolfgang Fischle

Max-Planck Institute for Biophysical Chemistry; Göttingen, Germany

Christian Seiser