Identification of a Human Histone Acetyltransferase Related to Monocytic Leukemia Zinc Finger Protein

• Published in: The Journal of biological chemistry Vol. 274; no. 40; pp. 28528 - 28536
• Main Authors: Champagne, Nathalie, Bertos, Nicholas R., Pelletier, Nadine, Wang, Audrey H., Vezmar, Marko, Yang, Yan, Heng, Henry H., Yang, Xiang-Jiao
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01-10-1999; American Society for Biochemistry and Molecular Biology
• Subjects: 3T3 Cells; Acetyltransferases - chemistry; Acetyltransferases - genetics; Acetyltransferases - metabolism; Adult; Amino Acid Sequence; Animals; Cell Line; chromosome 10; Chromosome Mapping; Chromosomes, Human, Pair 10; Cloning, Molecular; DNA, Complementary; Histone Acetyltransferases; Humans; Mice; Molecular Sequence Data; monocytic leukemia zinc finger protein-related factor; MORF protein; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Substrate Specificity
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.274.40.28528

We describe here the identification and functional characterization of a novel human histone acetyltransferase, termed MORF (monocytic leukemia zinc finger protein-related factor). MORF is a 1781-residue protein displaying significant sequence similarity to MOZ (monocytic leukemia zinc finger protein). MORF is ubiquitously expressed in adult human tissues, and its gene is located at human chromosome band 10q22. MORF has intrinsic histone acetyltransferase activity. In addition to its histone acetyltransferase domain, MORF possesses a strong transcriptional repression domain at its N terminus and 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 transcription.