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I Kitabayashi1, Y Aikawa1, A Yokoyama1, F Hosoda1, M Nagai2, N Kakazu3, T Abe3 & M Ohki1
1Cancer Genomics Division, National Cancer Center Research Institute, Tokyo, Japan
2First Department of Internal Medicine, Kagawa Medical School, Kagawa, Japan
3Department of Hygiene, Kyoto Prefectural University of Medicine, Kyoto, Japan
Correspondence to: I Kitabayashi, Cancer Genomics Division, National Cancer Center Research Institute, 5–1-1 Tsukiji, Chuo-ku, Tokyo 104–0045, Japan; Fax: 81–3-3542–0688
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Histone acetyltransferase p300 functions as a transcriptional co-activator which interacts with a number of transcription factors. Monocytic leukemia zinc finger protein (MOZ) has histone acetyltransferase activity. We report the fusion of the MOZ gene to the p300 gene in acute myeloid leukemia with translocation t(8;22)(p11;q13). FISH and Southern blot analyses showed the rearrangement of the MOZ and p300 genes. We determined the genomic structure of the p300 and the MOZ genes and the breakpoints of the translocation. Analysis of fusion transcripts indicated that the zinc finger and acetyltransferase domains of MOZ are fused to a largely intact p300. These results suggest that MOZ-p300, which has two acetyltransferase domains, could be involved in leukemogenesis through aberrant regulation of histone acetylation. Leukemia (2001) 15, 89–94.
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