2005 Volume 51 Issue 2 Pages 253-256
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.
