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Vol. 15, No. 6, pp. 774-788, March 15, 2001
1 Department of Molecular Biophysics and Biochemistry, Yale
University, Howard Hughes Medical Institute, New Haven, Connecticut
06536, USA; 2 Department of Biochemistry, University of
Cambridge, Cambridge CB2 1GA, UK
An in vitro system that recapitulates the in vivo effect of AU-rich
elements (AREs) on mRNA deadenylation has been developed from
Xenopus activated egg extracts. ARE-mediated deadenylation is
uncoupled from mRNA body decay, and the rate of deadenylation increases
with the number of tandem AUUUAs. A novel ARE-binding protein called
ePAB (for embryonic
poly(A)-binding protein) has been
purified from this extract by ARE affinity selection. ePAB exhibits
72% identity to mammalian and Xenopus PABP1 and is the predominant poly(A)-binding protein expressed in the stage VI oocyte
and during Xenopus early development. Immunodepletion of ePAB
increases the rate of both ARE-mediated and default deadenylation in
vitro. In contrast, addition of even a small excess of ePAB inhibits
deadenylation, demonstrating that the ePAB concentration is critical
for determining the rate of ARE-mediated deadenylation. These data
argue that ePAB is the poly(A)-binding protein responsible for
stabilization of poly(A) tails and is thus a potential regulator of
mRNA deadenylation and translation during early development.
[Key Words: In vitro deadenylation; AU-rich elements; development; mRNA stability; poly(A) tail]
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