Nucleic Acids Research, Vol 27, Issue 18 3752-3761, Copyright © 1999 by Oxford University Press
PS Knoepfler, DA Bergstrom, T Uetsuki, I Dac-Korytko, YH Sun, WE Wright, SJ Tapscott and MP Kamps
The t(1;19) chromosomal translocation of pediatric pre-B cell leukemia
produces chimeric oncoprotein E2a-Pbx1, which contains the N-terminal
transactivation domain of the basic helix-loop-helix (bHLH) transcription
factor, E2a, joined to the majority of the homeodomain protein, Pbx1. There
are three Pbx family members, which bind DNA as heterodimers with both
broadly expressed Meis/Prep1 homeo-domain proteins and specifically
expressed Hox homeodomain proteins. These Pbx heterodimers can augment the
function of transcriptional activators bound to adjacent elements. In
heterodimers, a conserved tryptophan motif in Hox proteins binds a pocket
on the surface of the Pbx homeodomain, while Meis/Prep1 proteins bind an
N-terminal Pbx domain, raising the possibility that the
tryptophan-interaction pocket of the Pbx component of a Pbx-Meis/Prep1
complex is still available to bind trypto-phan motifs of other
transcription factors bound to flanking elements. Here, we report that
Pbx-Meis1/Prep1 binds DNA cooperatively with heterodimers of E2a and MyoD,
myogenin, Mrf-4 or Myf-5. As with Hox proteins, a highly conserved
tryptophan motif N-terminal to the DNA- binding domains of each myogenic
bHLH family protein is required for cooperative DNA binding with
Pbx-Meis1/Prep1. In vivo, MyoD requires this tryptophan motif to evoke
chromatin remodeling in the Myogenin promoter and to activate Myogenin
transcription. Pbx-Meis/Prep1 complexes, therefore, have the potential to
cooperate with the myogenic bHLH proteins in regulating gene transcription.
ARTICLES
A conserved motif N-terminal to the DNA-binding domains of myogenic bHLH transcription factors mediates cooperative DNA binding with pbx- Meis1/Prep1
Department of Basic Science, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.
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