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Papers In Press, published online ahead of print August 28, 2005
Max-Planck Institute, Freiburg 79108
Corresponding Author: schneiderr{at}immunbio.mpg.de
Histone lysine methylation can have positive or negative effects on transcription, depending on the precise methylation site. According to the "histone code" hypothesis these methylation marks can be read by proteins that bind them specifically and then regulate downstream events. Hetero-chromatin Protein 1 (HP1), an essential component of heterochromatin, binds specifically to methylated lysine 9 of histone H3 (K9/H3). The linker histone H1.4 is methylated on K26 but the role of this methylation in downstream events remains unknown. Here we identify HP1 as a protein specifically recognising and binding to methylated K26/H1.4. We demonstrate that the Chromo domain of HP1 is mediating this binding and that phosphorylation of S27/H1.4 prevents HP1 from binding. We suggest that methylation of K26/H1.4 could have a role in tethering HP1 to chromatin and that this could also explain how HP1 is targeted to those regions of chromatin where it does not colocalise with methylated K9/H3. Our results provide the first experimental evidence for a "phospho switch" model in which neighbouring phosphorylation reverts the effect of histone lysine methylation.
J. Biol. Chem, 10.1074/jbc.C500229200
Submitted on June 1, 2005
Accepted on August 28, 2005
HP1 binds specifically to K26 methylated histone H1.4, whereas simultaneous S27 phosphorylation blocks HP1 binding
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