Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo.
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.
Aihara
Hitoshi
H
Department of Biochemistry, Nagasaki University School of Medicine, Nagasaki 852-8523, Japan.
Nakagawa
Takeya
T
Yasui
Kiyoshi
K
Ohta
Tsutomu
T
Hirose
Susumu
S
Dhomae
Naoshi
N
Takio
Koji
K
Kaneko
Mayumi
M
Takeshima
Yukio
Y
Muramatsu
Masami
M
Ito
Takashi
T
D000595:Amino Acid Sequence; D000818:Animals; D004330:Drosophila / Q000196:embryology / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008938:Mitosis / Q000502:physiology*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D006656:Protamine Kinase / Q000302:isolation & purification / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism*
D006657:Histones; D013912:Threonine; D006656:Protamine Kinase