MOZ (monocytic leukemia zinc finger protein) is a chromatin-associated histone acetyltransferase (HAT) that regulates chromatin remodeling and transcription. The MOZ gene was initially isolated as a consequence of two variant translocations that were identified in a distinct subtype of acute myeloid leukemias and resulted in the formation of MOZ fusion proteins. These fusions involve the HAT domain of MOZ with the activation domain of either transcriptional coactivator protein TIF2/GRIP1 or CBP, and lead to enhanced transcriptional activation by a mechanism involving aberrant histone acetylation. Additional MOZ related proteins, including MORF (MOZ related factor) and TIP60 (TAT interacting proteins 60), share significant similarities with MOZ including the putuative HAT domain. MORF also contains a strong transcriptional repression domain at its N terminus and a highly potent activation domain at the C terminus, suggesting that MORF has both HAT activity and contributes to the regulation of transcriptional activation. TIP60 was originally identified as a coactivator for the HIV TAT protein and also functions as a nuclear hormone receptor coactivator that enhances ligand dependent steroid receptor-mediated transactivation involving the androgen, estrogen and progesterone receptors.
