Journal of Biological Chemistry · 1999 · 172 citations · 43 references
Life SciencesMolecular BiologyMolecular GeneticsChromatin BiologyGene ExpressionTranscriptional RegulationChromatinHistone ModificationsHistone ProteinsFunctional Analysis Of Protein DomainsHistone AcetylationSequence SimilarityTranscriptional RepressionTranscriptional Repression ElementsZinc Finger DomainsZinc Finger ProteinsZinc Finger Transcription Factors
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.
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Crystal structure of the nucleosome core particle at 2.8 Å resolution
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