Title of article
A Posttermination Ribosomal Complex Is the Guanine Nucleotide Exchange Factor for Peptide Release Factor RF3
Author/Authors
Andrey V. Zavialov، نويسنده , , Richard H. Buckingham، نويسنده , , M?ns Ehrenberg، نويسنده ,
Issue Information
هفته نامه با شماره پیاپی سال 2001
Pages
10
From page
115
To page
124
Abstract
The mechanism by which peptide release factor RF3 recycles RF1 and RF2 has been clarified and incorporated in a complete scheme for translation termination. Free RF3 is in vivo stably bound to GDP, and ribosomes in complex with RF1 or RF2 act as guanine nucleotide exchange factors (GEF). Hydrolysis of peptidyl-tRNA by RF1 or RF2 allows GTP binding to RF3 on the ribosome. This induces an RF3 conformation with high affinity for ribosomes and leads to rapid dissociation of RF1 or RF2. Dissociation of RF3 from the ribosome requires GTP hydrolysis. Our data suggest that RF3 and its eukaryotic counterpart, eRF3, have mechanistic principles in common.
Journal title
CELL
Serial Year
2001
Journal title
CELL
Record number
1017535
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