The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase.
EVI-1 and its variant form, MDS1/EVI1, have been reported to act in an antagonistic manner and be differentially regulated in samples from patients with acute myeloid leukaemia and rearrangements of the long arm of chromosome 3. Here, we show that both EVI-1 and MDS1/EVI1 can repress transcription from a reporter construct containing EVI-1 binding sites and interact with histone deacetylase in mammalian cells. This interaction can be recapitulated in vitro and is mediated by a previously characterized transcription repression domain, whose activity is alleviated by the histone deacetylase inhibitor trichostatin A.
Vinatzer
U
U
Institut für Medizinische Biologie der Universitaet Wien, Wien, Austria.
Taplick
J
J
Seiser
C
C
Fonatsch
C
C
Wieser
R
R
D000818:Animals; D019556:COS Cells; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000378:metabolism*; D018274:Electroporation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005260:Female; D015321:Gene Rearrangement; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism*; D006801:Humans; D006877:Hydroxamic Acids / Q000494:pharmacology; D007938:Leukemia / Q000378:metabolism*; D000074008:MDS1 and EVI1 Complex Locus Protein; D015514:Oncogene Proteins, Fusion; D011247:Pregnancy; D011519:Proto-Oncogenes; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D014157:Transcription Factors; D014158:Transcription, Genetic / Q000187:drug effects
D004268:DNA-Binding Proteins; D004791:Enzyme Inhibitors; D056572:Histone Deacetylase Inhibitors; D006877:Hydroxamic Acids; D000074008:MDS1 and EVI1 Complex Locus Protein; C098704:MDS1-EVI1 fusion protein, human; C063575:MECOM protein, human; D015514:Oncogene Proteins, Fusion; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; C012589:trichostatin A; D006655:Histone Deacetylases