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Functional interplay of histone H1 phosphorylation and methylation
Author(s) -
Juan LiJung
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.544.1
Subject(s) - chromatin , mitosis , phosphorylation , histone , microbiology and biotechnology , histone methyltransferase , histone h1 , biology , histone methylation , crosstalk , methylation , methyltransferase , chemistry , biochemistry , dna methylation , dna , gene expression , gene , physics , optics
Functions of histone H1 modifications are largely unknown. Our mass spectrometry analysis reveals many novel H1 modification sites, some of which are cancer cell‐specific or deregulated by oncoproteins E6 or E7 of the human papillomavirus. We identified SET7 (also named SET7/9) as a novel histone methyltransferase for H1 at K33 in vitro and in vivo. This methylation can be enhanced by E6 or E7. Moreover, we found that H1 can also be phosphorylated at S35 and it occurs exclusively at mitosis. Interestingly, H1 phosphorylated at S35 is excluded from the condensed chromatin. Further investigation shows that PKA is the major kinase for mitotic H1S35 phosphorylation. Inhibition of PKA activity altered compactness of mitotic chromatin, implying that PKA‐mediated H1S35 phosphorylation during mitosis could be involved in mitotic compaction of chromatin. In addition, a crosstalk between K33 methylation and S35 phosphorylation was observed, suggesting a functional link between these two H1 PTMs.