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

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.

Publication types

  • Case Reports

MeSH terms

  • Acetyltransferases / genetics*
  • Cell Cycle Proteins / genetics*
  • Chromosomes, Human, Pair 22*
  • Chromosomes, Human, Pair 8*
  • Histone Acetyltransferases
  • Humans
  • Leukemia, Monocytic, Acute / genetics*
  • Leukemia, Monocytic, Acute / pathology
  • Male
  • Middle Aged
  • Oncogene Proteins, Fusion
  • Transcription Factors
  • Translocation, Genetic*
  • p300-CBP Transcription Factors


  • Cell Cycle Proteins
  • Oncogene Proteins, Fusion
  • Transcription Factors
  • Acetyltransferases
  • Histone Acetyltransferases
  • KAT6A protein, human
  • p300-CBP Transcription Factors
  • p300-CBP-associated factor