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

• Published in: Leukemia Vol. 15; no. 1; pp. 89 - 94
• Main Authors: KITABAYASHI, I, AIKAWA, Y, YOKOYAMA, A, HOSODA, F, NAGAI, M, KAKAZU, N, ABE, T, OHKI, M
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 2001; Nature Publishing Group
• Subjects: Acetyltransferases - genetics; Biological and medical sciences; Cell Cycle Proteins - genetics; chromosome 22; chromosome 8; Chromosomes, Human, Pair 22; Chromosomes, Human, Pair 8; Hematologic and hematopoietic diseases; Histone Acetyltransferases; Humans; Leukemia, Monocytic, Acute - genetics; Leukemia, Monocytic, Acute - pathology; Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis; Male; Medical sciences; Middle Aged; MOZ protein; Oncogene Proteins, Fusion; p300 protein; p300-CBP Transcription Factors; Transcription Factors; Translocation, Genetic; Chromosomal aberration; Human; Acyltransferases; Monocytic leukemia; Breakpoint; Enzyme; Pathogenesis; Transferases; Acute; Malignant hemopathy; Carcinogenesis; Histone acetyltransferase; M4 acute myelocytic leukemia; EC 2.3.1.48; Abnormal chromosome C8; Abnormal chromosome G22; Cytogenetics; Abnormal chromosome; Genetics; Acetylation; Fusion protein; Hybrid gene; Acute myelocytic leukemia; Chromosome translocation
• ISSN: 0887-6924; 1476-5551
• 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.