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J.Health Sci., 51(2), 253-256, 2005
Cloning and Characterization of a cDNA Encoding the Histone
Acetyltransferase Monocytic Leukemia Zinc Finger Protein
(MOZ) in the Rat
Kumiko Ohta, Shigehiro Osada, Jun-ichi Nishikawa, and Tsutomu
Nishihara*
Laboratory of Environmental Biochemistry, Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamada-Oka, Suita,
Osaka 565-0871, Japan
Many DNA-binding transcription factors require
coactivators for their function. Some of these coactivators have histone acetyltransferase (HAT)
activity, which is important for transcription from
chromatin template. We cloned a cDNA encoding the rat
homolog of monocytic leukemia zinc finger protein (MOZ), a member of the MYST (MOZ, Ybf2/Sas3,
Sas2, and Tip60) acetyltransferase family. Rat MOZ
(rnMOZ) encoded 1998 amino acids and was composed
of 16 exons. Comparison of the rnMOZ and human MOZ amino acid sequences revealed 89% identity over
the whole sequence and 100% identity in the MYST region, which is essential for HAT activity. Further,
we identified physical interaction between rnMOZ and
basic leucine zipper (bZIP)-type DNA-binding proteins, including c-Jun and CCAAT/enhancer binding
proteins. This finding suggests that MOZ may function in multiple cellular processes through various
bZIP-type transcription factors.
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