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J Biol Chem, Vol. 275, Issue 20, 15498-15503, May 19, 2000
From the Department of Medicine, University of Washington,
Seattle, Washington 98195
The heterogeneous nuclear ribonucleoprotein
(hnRNP) K, a component of the hnRNP particles, appears to be
involved in several steps of regulation of gene expression. To gain
insight into mechanisms of K protein action, we performed two-hybrid
screens using full-length hnRNP K as a bait. Several novel protein
partners were identified, including Y-box-binding protein (YB-1),
splicing factors 9G8 and SRp20, DNA-methyltransferase, hnRNP L, and
hnRNP U. In vitro binding studies and
co-immunoprecipitation from cellular extracts provided evidence for
direct interaction between hnRNP K and YB-1. Two distinct domains in
YB-1 were responsible for binding to K protein. Each protein was able
to transactivate transcription from a polypyrimidine-rich promoter;
however, this effect was reduced when K and YB-1 proteins were
coexpressed suggesting a functional interaction between these two proteins.
Interaction of Two Multifunctional Proteins
HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K AND Y-BOX-BINDING
PROTEIN*
*
This work was supported by National Institutes of Health
Grants GM 45134 and DK 45978, the American Diabetes Association, and
the Northwest Kidney Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Medicine, Box
356521, University of Washington, Seattle, WA 98195. Tel.: 206-543-3792; Fax: 206-685-8661; E-mail:
karolb@u.washington.edu.
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