Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo

  1. Hitoshi Aihara1,
  2. Takeya Nakagawa1,
  3. Kiyoshi Yasui1,
  4. Tsutomu Ohta2,
  5. Susumu Hirose3,
  6. Naoshi Dhomae4,
  7. Koji Takio5,
  8. Mayumi Kaneko6,
  9. Yukio Takeshima6,
  10. Masami Muramatsu7, and
  11. Takashi Ito1,8
  1. 1Department of Biochemistry, Nagasaki University School of Medicine, Nagasaki, Nagasaki 852-8523, Japan; 2Medical Genomic Center, National Cancer Center Research Institute, Tokyo 104-0045, Japan; 3Department of Developmental Genetics, National Institute of Genetics, Shizuoka-ken 411-8540, Japan; 4The Institute of Physical and Chemical Research, Wako-shi, Saitama 351-0198, Japan; 5RIKEN Harima Institute, Mikazuki-cho, Hyogo 679-5148, Japan; 6Second Department of Pathology, Hiroshima University School of Medicine, Minami-ku, Hiroshima 734-8551, Japan; 7Saitama Medical School Research Center for Genomic Medicine, Hidaka, Saitama 350-1241, Japan

Abstract

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.

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Footnotes

  • Supplemental material is available at http://genesdev.org.

  • Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1184604.

  • ↵8 Corresponding author.

    ↵8 E-MAIL tito{at}net.nagasaki-u.ac.jp; FAX 81-95-849-7040.

    • Accepted March 15, 2004.
    • Received January 6, 2004.
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This Article

  1. Published in Advance April 12, 2004, doi: 10.1101/gad.1184604 Genes & Dev. 18: 877-888 Cold Spring Harbor Laboratory Press

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