Cloning and Characterization of a cDNA Encoding the Histone Acetyltransferase Monocytic Leukemia Zinc Finger Protein (MOZ) in the Rat

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  • Ohta Kumiko
    Laboratory of Environmental Biochemistry, Graduate School of Pharmaceutical Sciences, Osaka University
  • Osada Shigehiro
    Laboratory of Environmental Biochemistry, Graduate School of Pharmaceutical Sciences, Osaka University
  • Nishikawa Jun-ichi
    Laboratory of Environmental Biochemistry, Graduate School of Pharmaceutical Sciences, Osaka University
  • Nishihara Tsutomu
    Laboratory of Environmental Biochemistry, Graduate School of Pharmaceutical Sciences, Osaka University

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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. <br>

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