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J. Biol. Chem., Vol. 281, Issue 10, 6573-6580, March 10, 2006

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Histone H1 Phosphorylation Occurs Site-specifically during Interphase and Mitosis

IDENTIFICATION OF A NOVEL PHOSPHORYLATION SITE ON HISTONE H1^*

From the Division of Clinical Biochemistry, Biocenter, Innsbruck Medical University, Innsbruck A-6020, Austria

H1 histones, isolated from logarithmically growing and mitotically enriched human lymphoblastic T-cells (CCRF-CEM), were fractionated by reversed phase and hydrophilic interaction liquid chromatography, subjected to enzymatic digestion, and analyzed by amino acid sequencing and mass spectrometry. During interphase the four H1 subtypes present in these cells differ in their maximum phosphorylation levels: histone H1.5 is tri-, H1.4 di-, and H1.3 and H1.2, only monophosphorylated. The phosphorylation is site-specific and occurs exclusively on serine residues of SP(K/A)K motifs. The phosphorylation sites of histone H1.5 from mitotically enriched cells were also examined. In contrast to the situation in interphase, at mitosis there were additional phosphorylations, exclusively at threonine residues. Whereas the tetraphosphorylated H1.5 arises from the triphosphosphorylated form by phosphorylation of one of two TPKK motifs in the C-terminal domain, namely Thr¹³⁷ and Thr¹⁵⁴, the pentaphosphorylated H1.5 was the result of phosphorylation of one of the tetraphosphorylated forms at a novel nonconsensus motif at Thr¹⁰ in the N-terminal tail. Despite the fact that histone H1.5 has five (S/T)P(K/A)K motifs, all of these motifs were never found to be phosphorylated simultaneously. Our data suggest that phosphorylation of human H1 variants occurs nonrandomly during both interphase and mitosis and that distinct serine- or threonine-specific kinases are involved in different cell cycle phases. The order of increased phosphorylation and the position of modification might be necessary for regulated chromatin decondensation, thus facilitating processes of replication and transcription as well as of mitotic chromosome condensation.

Received for publication, August 15, 2005 , and in revised form, December 21, 2005.

^* This work, as part of the European Science Foundation EUROCORES Programme Euro-DYNA, was supported by funds from the Austrian Science Foundation Project I23-B03. 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.

¹ To whom correspondence should be addressed: Division of Clinical Biochemistry, Biocenter, Innsbruck Medical University, Fritz-Pregl-Strasse 3, Innsbruck A-6020, Austria. Tel.: 43-512-507-3521; Fax: 43-512-507-2876; E-mail: herbert.lindner{at}i-med.ac.at.

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