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(Received for publication, March 5, 1997, and in revised form, March 17, 1997)
From the Department of Biochemistry, University of Illinois,
Urbana, Illinois 61801
RNA-binding proteins containing KH domains are
widely distributed. One KH domain protein of unknown function, vigilin
(also known as the high density lipoprotein-binding protein), contains 14 KH domains and is ubiquitous in vertebrate cells. We previously used
RNA gel mobility shift assays to describe an estrogen-inducible protein
which binds specifically to a segment of the 3
Volume 272, Number 19,
Issue of May 9, 1997
pp. 12249-12252
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
-Untranslated
Region-binding Protein
-untranslated region
(3-UTR) of vitellogenin mRNA, an area which has been implicated in
the estrogen-mediated stabilization of vitellogenin mRNA. Here we
show that the vitellogenin mRNA-binding protein (VitRNABP) is
vigilin. The VitRNABP was isolated as a 150-155-kDa protein on a
vitellogenin mRNA 3-UTR affinity column. Peptide microsequencing revealed that the purified protein was vigilin, a conclusion confirmed in Western blot analysis with antibodies to vigilin. Direct
confirmation that vigilin is the VitRNABP was obtained from RNA gel
mobility shift assays which demonstrated that antibodies to chicken
vigilin supershifted the Xenopus VitRNABP band.
Xenopus liver vigilin mRNA and the VitRNABP exhibited
similar induction by estrogen, providing additional confirmation that
vigilin is the estrogen-inducible protein which binds to the 3-UTR of
estrogen-stabilized vitellogenin mRNA. These data support a role
for vigilin in the hormonal control of mRNA metabolism.
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