Re. Dodson et Dj. Shapiro, VIGILIN, A UBIQUITOUS PROTEIN WITH 14 K-HOMOLOGY DOMAINS, IS THE ESTROGEN-INDUCIBLE VITELLOGENIN MESSENGER-RNA 3'-UNTRANSLATED REGION-BINDING PROTEIN, The Journal of biological chemistry, 272(19), 1997, pp. 12249-12252
RNA-binding proteins containing KH domains are widely distributed. One
KH domain protein of unknown function, vigilin (also known as the hig
h density lipoprotein-binding protein), contains 14 KH domains and is
ubiquitous in vertebrate cells. We previously used RNA gel mobility sh
ift assays to describe an estrogen-inducible protein which binds speci
fically to a segment of the 3'-untranslated region (3'-UTR) of vitello
genin mRNA, an area which has been implicated in the estrogen-mediated
stabilization of vitellogenin mRNA, Here we show that the vitellogeni
n mRNA-binding protein (VitRNABP) is vigilin. The VitRNABP was isolate
d as a 150-155-kDa protein on a vitellogenin mRNA 3'-UTR affinity colu
mn. Peptide microsequencing revealed that the purified protein was vig
ilin, a conclusion confirmed in Western blot analysis with antibodies
to vigilin. Direct confirmation that vigilin is the VitRNABP was obtai
ned from RNA gel mobility shift assays which demonstrated that antibod
ies to chicken vigilin supershifted the Xenopus VitRNABP band. Xenopus
liver vigilin mRNA and the VitRNABP exhibited similar induction by es
trogen, providing additional confirmation that vigilin is the estrogen
-inducible protein which binds to the 3'-UTR of estrogen-stabilized vi
tellogenin mRNA. These data support a role for vigilin in the hormonal
control of mRNA metabolism.