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RESEARCH PAPER
1 Department of Biochemistry, Nagasaki University School of Medicine, Nagasaki, Nagasaki 852-8523, Japan; 2 Medical Genomic Center, National Cancer Center Research Institute, Tokyo 104-0045, Japan; 3 Department of Developmental Genetics, National Institute of Genetics, Shizuoka-ken 411-8540, Japan; 4 The Institute of Physical and Chemical Research, Wako-shi, Saitama 351-0198, Japan; 5 RIKEN Harima Institute, Mikazuki-cho, Hyogo 679-5148, Japan; 6 Second Department of Pathology, Hiroshima University School of Medicine, Minami-ku, Hiroshima 734-8551, Japan; 7 Saitama Medical School Research Center for Genomic Medicine, Hidaka, Saitama 350-1241, Japan
Posttranslational histone modifications are important for the regulation of many biological phenomena. Here, we show the purification and characterization of nucleosomal histone kinase-1 (NHK-1). NHK-1 has a high affinity for chromatin and phosphorylates a novel site, Thr 119, at the C terminus of H2A. Notably, NHK-1 specifically phosphorylates nucleosomal H2A, but not free H2A in solution. In Drosophila embryos, phosphorylated H2A Thr 119 is found in chromatin, but not in the soluble core histone pool. Immunostaining of NHK-1 revealed that it goes to chromatin during mitosis and is excluded from chromatin during S phase. Consistent with the shuttling of NHK-1 between chromatin and cytoplasm, H2A Thr 119 is phosphorylated during mitosis but not in S phase. These studies reveal that NHK-1-catalyzed phosphorylation of a conserved serine/threonine residue in H2A is a new component of the histone code that might be related to cell cycle progression.
[Keywords: Nucleosome; phosphorylation; histone code; transcription; NHK-1]
Received January 6, 2004; revised version accepted March 15, 2004.
Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1184604.
E-MAIL tito{at}net.nagasaki-u.ac.jp; FAX 81-95-849-7040.
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