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J. Biol. Chem., Vol. 280, Issue 45, 38090-38095, November 11, 2005

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HP1 Binds Specifically to Lys²⁶-methylated Histone H1.4, whereas Simultaneous Ser²⁷ Phosphorylation Blocks HP1 Binding^*

Sylvain Daujat1, Ulrike Zeissler1, Tanja Waldmann, Nicole Happel, and Robert Schneider2

From the Max Planck Institute for Immunobiology, 79108 Freiburg, Germany and the Institute for Biochemistry and Molecular Cell Biology, University of Goettingen, 37073 Goettingen, Germany

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 Lys⁹ of histone H3 (K9/H3). The linker histone H1.4 is methylated on Lys²⁶ (K26/H1.4), but the role of this methylation in downstream events remains unknown. Here we identify HP1 as a protein specifically recognizing and binding to methylated K26/H1.4. We demonstrate that the Chromo domain of HP1 is mediating this binding and that phosphorylation of Ser²⁷ on H1.4 (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 colocalize with methylated K9/H3. Our results provide the first experimental evidence for a "phospho switch" model in which neighboring phosphorylation reverts the effect of histone lysine methylation.

Received for publication, June 1, 2005 , and in revised form, August 19, 2005.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ These authors contributed equally to this work.

² Supported by a Human Frontier Science Program career development award. To whom correspondence should be addressed. Tel.: 49-761-51080; Fax: 49-761-5108220; E-mail: schneiderr{at}immunbio.mpg.de.

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