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Papers In Press, published online ahead of print October 14, 2002
J. Biol. Chem, 10.1074/jbc.M203029200
Submitted on March 28, 2002
Revised on October 10, 2002
Accepted on October 14, 2002
Department of Physiological Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033
Corresponding Author: hoshino{at}mol.f.u-tokyo.ac.jp
The mammalian GSPT, which consists of amino-terminal (N) and carboxy-terminal (C) domains, functions as the eukaryotic releasing factor 3 (eRF3) by interacting with eRF1 in translation termination. This function requires only the C-domain that is homologous to the elongation factor (EF) 1a, while the N-domain interacts with poly-adenylate binding protein (PABP) which binds the poly(A) tail of mRNA and associates with the eukaryotic initiation factor (eIF) 4G. Here we describe a novel role of GSPT in translation. We first determined an amino-acid sequence required for the PABP interaction in the N-domain. Inhibition of this interaction significantly attenuated translation of capped/poly(A)-tailed mRNA not only in an in vitro translation system but also in living cells. There was a PABP-dependent linkage between the termination factor complex eRF1–GSPT and the initiation factor eIF4G associating with 5’ cap through eIF4E. Although the inhibition of the GSPT–PABP interaction did not affect the de novo formation of 80S ribosomal initiation complex, it appears to suppress the subsequent recycle of ribosome. These results indicate that GSPT/eRF3 plays an important role in translation cycle through the interaction with PABP, in addition to mediating the termination with eRF1.
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