Nucleic Acids Research, Vol 24, Issue 19 3821-3828, Copyright © 1996 by Oxford University Press
B Funke, B Zuleger, R Benavente, T Schuster, M Goller, J Stevenin and I Horak
The murine poly(C)-binding protein (mCBP) was previously shown to belong to
the group of K-homology (KH) proteins by virtue of its homology to hnRNP-K.
We have isolated cDNA-splice variants of mCBP which differ by two variable
regions of 93 bp and/or 39 +/- 3 bp respectively. Both variable regions are
located between the second and third KH-domain of mCBP. The
characterization of a partial genomic clone enabled us to propose a model
for the generation of the second variable region by the use of a putative
alternative splice signal. The mCBP mRNA is expressed ubiquitously and the
protein is found predominantly in the nucleus with the exception of the
nucleoli. We have identified five proteins which interact with mCBP in the
yeast two hybrid system: mouse y-box protein 1 (msy-1), y-box-binding
protein, hnRNP-L, filamin and splicing factor 9G8. The interaction between
mCBP and splicing factor 9G8 was confirmed in vivo. These results suggest a
function of mCBP in RNA metabolism.
ARTICLES
The mouse poly(C)-binding protein exists in multiple isoforms and interacts with several RNA-binding proteins
Institut fur Virologie und Immunbiologie der Universitat Wurzburg, Germany.
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