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Bromodomain and histone acetyltransferase domain specificities control mixed lineage leukemia phenotype
Journal article   Open access   Peer reviewed

Bromodomain and histone acetyltransferase domain specificities control mixed lineage leukemia phenotype

Donna A Santillan, Catherine M Theisler, Amanda S Ryan, Relja Popovic, Tara Stuart, Ming-Ming Zhou, Serhan Alkan and Nancy J Zeleznik-Le
Cancer research (Chicago, Ill.), Vol.66(20), pp.10032-10039
10/15/2006
DOI: 10.1158/0008-5472.CAN-06-2597
PMID: 17047066
url
https://doi.org/10.1158/0008-5472.CAN-06-2597View
Published (Version of record) Open Access

Abstract

A critical unanswered question about mixed lineage leukemia (MLL) is how specific MLL fusion partners control leukemia phenotype. The MLL-cyclic AMP-responsive element binding protein-binding protein (CBP) fusion requires both the CBP bromodomain and histone acetyltransferase (HAT) domain for transformation and causes acute myelogenous leukemia (AML), often preceded by a myelodysplastic phase. We did domain-swapping experiments to define whether unique specificities of these CBP domains drive this specific MLL phenotype. Within MLL-CBP, we replaced the CBP bromodomain or HAT domain with P300/CBP-associated factor (P/CAF) or TAF(II)250 bromodomains or the P/CAF or GCN5 HAT domains. HAT, but not bromodomain, substitutions conferred enhanced proliferative capacity in vitro but lacked expression of myeloid cell surface markers normally seen with MLL-CBP. Mice reconstituted with domain-swapped hematopoietic progenitors developed different disease from those with MLL-CBP. This included development of lymphoid disease and lower frequency of the myelodysplastic phase in those mice developing AML. We conclude that both the CBP bromodomain and HAT domain play different but critical roles in determining the phenotype of MLL-CBP leukemia. Our results support an important role for MLL partner genes in determining the leukemia phenotype besides their necessity in leukemogenesis. Here, we find that subtleties in MLL fusion protein domain specificity direct cells toward a specific disease phenotype.
Phenotype Myeloid-Lymphoid Leukemia Protein - metabolism Leukemia - pathology p300-CBP Transcription Factors - physiology Histone Acetyltransferases - genetics Molecular Sequence Data Substrate Specificity Myeloid-Lymphoid Leukemia Protein - physiology p300-CBP Transcription Factors - genetics Cell Transformation, Neoplastic - genetics Histone Acetyltransferases - metabolism Leukemia - genetics Protein Structure, Tertiary Amino Acid Sequence Leukemia - enzymology Mice, Inbred C57BL Hematopoietic Stem Cells - metabolism Histone Acetyltransferases - physiology Cell Transformation, Neoplastic - metabolism p300-CBP Transcription Factors - metabolism Animals Myeloid-Lymphoid Leukemia Protein - genetics Hematopoietic Stem Cells - cytology Mice Hematopoietic Stem Cells - enzymology

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