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J Biol Chem, Vol. 274, Issue 24, 16677-16680, June 11, 1999
From the Department of Physiological Chemistry, Graduate School of
Pharmaceutical Sciences, University of Tokyo,
Tokyo 113-0033, Japan
The mammalian GTP-binding protein GSPT, whose
carboxyl-terminal sequence is homologous to the eukaryotic elongation
factor EF1
, binds to the polypeptide chain releasing factor eRF1 to function as eRF3 in the translation termination. The amino-terminal domain of GSPT was, however, not required for the binding. Search for
other GSPT-binding proteins in yeast two-hybrid screening system
resulted in the identification of a cDNA encoding
polyadenylate-binding protein (PABP), whose amino terminus is
associating with the poly(A) tail of mRNAs presumably for their
stabilization. The interaction appeared to be mediated through the
carboxyl-terminal domain of PABP and the amino-terminal region of GSPT.
Interestingly, multimerization of PABP with poly(A), which is ascribed
to the action of its carboxyl-terminal domain, was completely inhibited
by the interaction with the amino-terminal domain of GSPT. These
results indicate that GSPT/eRF3 may play important roles not only in
the termination of protein synthesis but also in the regulation of
mRNA stability. Thus, the present study is the first report
showing that GSPT/eRF3 carries the translation termination signal to
3'-poly(A) tail ubiquitously present in eukaryotic mRNAs.
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