eIF2A, an initiator tRNA carrier refractory to eIF2 kinases, functions synergistically with eIF5B

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The initiator tRNA (Met-tRNA(i)(Met)) at the P site of the small ribosomal subunit plays an important role in the recognition of an mRNA start codon. In bacteria, the initiator tRNA carrier, IF2, facilitates the positioning of Met-tRNAiMet on the small ribosomal subunit. Eukarya contain the Met-tRNAiMet carrier, eIF2 (unrelated to IF2), whose carrier activity is inhibited under stress conditions by the phosphorylation of its -subunit by stress-activated eIF2 kinases. The stress-resistant initiator tRNA carrier, eIF2A, was recently uncovered and shown to load Met-tRNAiMet on the 40S ribosomal subunit associated with a stress-resistant mRNA under stress conditions. Here, we report that eIF2A interacts and functionally cooperates with eIF5B (a homolog of IF2), and we describe the functional domains of eIF2A that are required for its binding of Met-tRNAiMet, eIF5B, and a stress-resistant mRNA. The results indicate that the eukaryotic eIF5B-eIF2A complex functionally mimics the bacterial IF2 containing ribosome-, GTP-, and initiator tRNA-binding domains in a single polypeptide.
Publisher
SPRINGER BASEL AG
Issue Date
2018-12
Language
English
Article Type
Article
Citation

CELLULAR AND MOLECULAR LIFE SCIENCES, v.75, no.23, pp.4287 - 4300

ISSN
1420-682X
DOI
10.1007/s00018-018-2870-4
URI
http://hdl.handle.net/10203/251658
Appears in Collection
BS-Journal Papers(저널논문)
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