Kitabayashi I, Aikawa Y, Yokoyama A, Hosoda F, Nagai M, Kakazu N, Abe T, Ohki M
Cancer Genomics Division, National Cancer Center Research Institute, Tokyo, Japan.
Leukemia. 2001 Jan;15(1):89-94. doi: 10.1038/sj.leu.2401983.
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.
组蛋白乙酰转移酶p300作为一种转录共激活因子，可与多种转录因子相互作用。单核细胞白血病锌指蛋白（MOZ）具有组蛋白乙酰转移酶活性。我们报告了在急性髓系白血病中，MOZ基因与p300基因发生融合，并伴有t(8;22)(p11;q13)易位。荧光原位杂交（FISH）和Southern印迹分析显示MOZ和p300基因发生了重排。我们确定了p300和MOZ基因的基因组结构以及易位的断点。融合转录本分析表明，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。这些结果提示，具有两个乙酰转移酶结构域的MOZ-p300可能通过对组蛋白乙酰化的异常调节参与白血病的发生。
