January 2001, Volume 15, Issue 1, Pages 89 - 94

Original Manuscript

Fusion of MOZ and p300 histone acetyltransferases in acute monocytic leukemia with a t(8;22)(p11;q13) chromosome translocation 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

Keywords

chromosome translocation;   histone acetylation;   acute myeloid leukemia;   MOZ;   p300

Abstract

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.

Received 12 July 2000; Accepted 11 September 2000

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