Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein

We describe here the identification and functional characterization of a no vel human histone acetyltransferase, termed MORF (monocytic leukemia zinc f inger protein-related factor). MORF is a 1781-residue protein displaying si gnificant sequence similarity to MOZ (monocytic leukemia zinc finger protei n). MORF is ubiquitously expressed in adult human tissues, and its gene is located at human chromosome band 10q22. MORF has intrinsic histone acetyltr ansferase activity. in addition to its histone acetyltransferase domain, MO RF possesses a strong transcriptional repression domain at its N terminus a nd a highly potent activation domain at its C terminus. Therefore, MORF is a novel histone acetyltransferase that contains multiple functional domains and may be involved in both positive and negative regulation of transcript ion.