Portal de Periódicos da CAPES

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

1999; Elsevier BV; Volume: 274; Issue: 40 Linguagem: Inglês

10.1074/jbc.274.40.28528

1083-351X

Nathalie Champagne, Nicholas Bertos, Nadine Pelletier, Audrey H. Wang, Marko Vezmar, Yan Yang, Henry H.Q. Heng, Xiang-Jiao Yang,

Protein Degradation and Inhibitors

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.