Nucleic Acids Research, Vol 24, Issue 11 2112-2118, Copyright © 1996 by Oxford University Press
MA Vigano and LM Staudt
Oct-3, a member of the POU family of transcription factors, is expressed in
pluripotent cells of early mammalian embryos and in undifferentiated
embryonal carcinoma cell lines. Using a variety of Oct- 3 mutants, we have
identified two different domains of Oct-3 which activate transcription in
transfected mammalian cells. One of these domains, located in the
C-terminal part of the protein, plays a major role in transcriptional
activation when Oct-3 is bound to its cognate site, the octamer motif. An
Oct-3 mutant containing a single amino acid substitution in the POU
homeodomain is unable to bind the octamer target in vitro, yet is still
able to activate transcription in an octamer-dependent manner. We provide
evidence that transactivation by this mutant involves protein-protein
interactions with the ubiquitous octamer binding factor Oct-1. This
interaction requires the POU- specific domain of Oct-3 and allows
recruitment of Oct-3 to the target promoter even in the absence of Oct-3
DNA binding.
ARTICLES
Transcriptional activation by Oct-3: evidence for a specific role of the POU-specific domain in mediating functional interaction with Oct-1
DIBIT-Istituto Scientifico H.S. Raffaele, Milano, Italy.
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