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.
journal_name
Proc Natl Acad Sci U S Aauthors
Kurata S,Nielsen KH,Mitchell SF,Lorsch JR,Kaji A,Kaji Hdoi
10.1073/pnas.1006247107subject
Has Abstractpub_date
2010-06-15 00:00:00pages
10854-9issue
24eissn
0027-8424issn
1091-6490pii
1006247107journal_volume
107pub_type
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