Nucleic Acids Research, Vol 25, Issue 12 2284-2292, Copyright © 1997 by Oxford University Press
YS Yang, MC Yang, PW Tucker and JD Capra
NonO is an unusual nucleic acid binding protein not only in that it binds
both DNA and RNA but that it does so via functionally separable domains.
Here we document that NonO enhances the binding of some (E47, OTF-1 and
OTF-2) but not all (PEA3) conventional sequence-specific transcription
factors to their recognition sites in artificial substrates as well as in
an immunoglobulin VHpromoter. We also show that NonO induces the binding of
the Ku complex to DNA ends. Ku has no known DNA sequence specificity. These
enhancement of binding effects are NonO concentration dependent. Using the
E box activity of E47 as a model, kinetic studies demonstrate that the
association rate of the protein-DNA complex increases in the presence of
NonO while the dissociation rate remains the same, thereby increasing the
sum total of the interaction. Oligo competition experiments indicate that
NonO does not contact the target DNA in order to enhance the binding
activity of DNA binding proteins. Rather, methylation interference analysis
reveals that the induced E47 binding-activity has the same DNA-binding
sequence specificity as the normal binding. This result suggests that one
of the effects of NonO is to induce a true protein-DNA interaction. In this
way, it might be possible for NonO to play a crucial role in gene
regulation.
ARTICLES
NonO enhances the association of many DNA-binding proteins to their targets
Molecular Immunology Center, Department of Microbiology, The University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75235-9140, USA.
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