Ribosome recycling step in yeast cytoplasmic protein synthesis is catalyzed by eEF3 and ATP.

Abstract:

:After each round of protein biosynthesis, the posttermination complex (PoTC) consisting of a ribosome, mRNA, and tRNA must be disassembled into its components for a new round of translation. Here, we show that a Saccharomyces cerevisiae model PoTC was disassembled by ATP and eukaryotic elongation factor 3 (eEF3). GTP or ITP functioned with less efficiency and adenosine 5gamma'-(beta,gamma-imido)triphosphate did not function at all. The k(cat) of eEF3 was 1.12 min(-1), which is comparable to that of the in vitro initiation step. The disassembly reaction was inhibited by aminoglycosides and cycloheximide. The subunits formed from the yeast model PoTC remained separated under ionic conditions close to those existing in vivo, suggesting that they are ready to enter the initiation process. Based on our experimental techniques used in this paper, the release of mRNA and tRNA and ribosome dissociation took place simultaneously. No 40S*mRNA complex was observed, indicating that eEF3 action promotes ribosome recycling, not reinitiation.

authors

Kurata S,Nielsen KH,Mitchell SF,Lorsch JR,Kaji A,Kaji H

doi

10.1073/pnas.1006247107

subject

Has Abstract

pub_date

2010-06-15 00:00:00

pages

10854-9

issue

24

eissn

0027-8424

issn

1091-6490

pii

1006247107

journal_volume

107

pub_type

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