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¹ Department of Applied Biology, and
² Insect Biomedical Research Center, and
³ Venture Laboratory, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
⁴ Experimental Research Center for Infectious Diseases, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan

G9a belongs to the subfamily of histone H3 lysine 9 (H3-K9)-specific methyltransferases. On amino acid sequence alignment of human and Drosophila G9a, we found that the N-terminal region from amino acids 532–605 to be evolutionarily conserved and named this the G9a homology domain (GHD). Using the GHD of human G9a (hG9a) as a bait, we isolated cDNA encoding a zinc finger protein 200 (ZNF200), which contains five C₂H₂-type zinc finger domains in tandem arrays. Interaction between G9a and ZNF200 could be demonstrated by in vitro binding assays and immunoprecipitation experiments using cultured human HEK293 cell extracts. GST pull-down assays using deletion derivatives of ZNF200 revealed that the interaction is through a region encompassing three of the five zinc finger domains. Furthermore, ZNF200 appear to co-localize with G9a in the nucleoplasm of HEK293 cells as discrete speckles. These results demonstrate that ZNF200 is a novel binding partner of G9a.

^aPresent address: Developmental Biology, Stanford School of Medicine, 279 Campus Dr. B371, Stanford, CA 94305, USA.

^* Correspondence: E-mail: myamaguc{at}kit.ac.jp

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				Y. Kato, M. Kato, M. Tachibana, Y. Shinkai, and M. Yamaguchi Characterization of Drosophila G9a in vivo and identification of genetic interactants Genes Cells, July 1, 2008; 13(7): 703 - 722. [Abstract] [Full Text] [PDF]