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Mol. Cell. Biol., Aug 1997, 4870-4876, Vol 17, No. 8
M Kiledjian, CT DeMaria, G Brewer and K Novick
mRNA turnover is an important regulatory component of gene expression and
is significantly influenced by ribonucleoprotein (RNP) complexes which form
on the mRNA. Studies of human alpha-globin mRNA stability have identified a
specific RNP complex (alpha-complex) which forms on the 3' untranslated
region (3'UTR) of the mRNA and appears to regulate the erythrocyte-specific
accumulation of alpha-globin mRNA. One of the protein activities in this
multiprotein complex is a poly(C)-binding activity which consists of two
proteins, alphaCP1 and alphaCP2. Neither of these proteins, individually or
as a pair, can bind the alpha-globin 3'UTR unless they are complexed with
the remaining non-poly(C) binding proteins of the alpha-complex. With the
yeast two-hybrid screen, a second alpha-complex protein was identified.
This protein is a member of the previously identified A+U-rich (ARE)
binding/degradation factor (AUF1) family of proteins, which are also known
as the heterogeneous nuclear RNP (hnRNP) D proteins. We refer to these
proteins as AUF1/hnRNP-D. Thus, a protein implicated in ARE-mediated mRNA
decay is also an integral component of the mRNA stabilizing alpha-complex.
The interaction of AUF1/hnRNP-D is more efficient with alphaCP1 relative to
alphaCP2 both in vitro and in vivo, suggesting that the alpha-complex might
be dynamic rather than a fixed complex. AUF1/hnRNP-D could, therefore, be a
general mRNA turnover factor involved in both stabilization and decay of
mRNA.
Copyright © 1997, American Society for Microbiology
Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the alpha-globin mRNA stability complex
Department of Cell, Developmental and Neurobiology, Rutgers University, Piscataway, New Jersey 08855, USA. kiledjia@biology.rutgers.edu
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