Fusion of MOZ and p300 histone acetyltransferases in acute monocytic leukemia with a t(8;22)(p11;q13) chromosome translocation
Fusion of MOZ and p300 histone acetyltransferases in acute monocytic leukemia with a t(8;22)(p11;q13) chromosome translocation
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DOI：
10.1038/sj.leu.2401983
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发表时间：
2001-01-01
期刊：
影响因子：
11.4
通讯作者：
Ohki, M
中科院分区：
文献类型：
--
作者：
Kitabayashi, I;Aikawa, Y;Ohki, M
组蛋白乙酰转移酶p300作为转录共激活因子与许多转录因子相互作用。单核细胞白血病锌指蛋白（MOZ）具有组蛋白乙酰转移酶活性。我们报告了急性髓性白血病伴t（8;22）（p11;q13）易位的MOZ基因与p300基因的融合。FISH和Southern杂交分析显示MOZ和p300基因重排。我们确定了p300和MOZ基因的基因组结构和易位的断点。融合转录本的分析表明MOZ的锌指结构域和乙酰转移酶结构域与基本完整的p300融合。这些结果表明MOZ-p300具有两个乙酰转移酶结构域。可能通过组蛋白乙酰化的异常调节参与白血病的发生。
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.