ArticleRNA (New York, N.Y.)2011
Structural integrity of {alpha}-helix H12 in translation initiation factor eIF5B is critical for 80S complex stability.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Role of aIF5B in archaeal translation initiation.Nucleic acids research · 2022Article
- Established and Emerging Regulatory Roles of Eukaryotic Translation Initiation Factor 5B (eIF5B).Frontiers in genetics · 2021Review
- Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex.Nature communications · 2020Article
- Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Recent Advances in Archaeal Translation Initiation.Frontiers in microbiology · 2020Review
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- eIF5 and eIF5B together stimulate 48S initiation complex formation during ribosomal scanning.Nucleic acids research · 2014Article
- Upregulation of eIF5B controls cell-cycle arrest and specific developmental stages.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA.Nature structural & molecular biology · 2014Article
- Poliovirus switches to an eIF2-independent mode of translation during infection.Journal of virology · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Translation initiation factor eIF5B promotes GTP-dependent ribosomal subunit joining in the final step of the translation initiation pathway. The protein resembles a chalice with the α-helix H12 forming the stem connecting the GTP-binding domain cup to the domain IV base. Helix H12 has been proposed to function as a rigid lever arm governing domain IV movements in response to nucleotide binding and as a molecular ruler fixing the distance between domain IV and the G domain of the factor. To investigate its function, helix H12 was lengthened or shortened by one or two turns. In addition, six consecutive residues in the helix were substituted by Gly to alter the helical rigidity. Whereas the mutations had minimal impacts on the factor's binding to the ribosome and its GTP binding and hydrolysis activities, shortening the helix by six residues impaired the rate of subunit joining in vitro and both this mutation and the Gly substitution mutation lowered the yield of Met-tRNA(i)(Met) bound to 80S complexes formed in the presence of nonhydrolyzable GTP. Thus, these two mutations, which impair yeast cell growth and enhance ribosome leaky scanning in vivo, impair the rate of formation and stability of the 80S product of subunit joining. These data support the notion that helix H12 functions as a ruler connecting the GTPase center of the ribosome to the P site where Met-tRNA(i)(Met) is bound and that helix H12 rigidity is required to stabilize Met-tRNA(i)(Met) binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.