ArticleNucleic acids research2014
Rps5-Rps16 communication is essential for efficient translation initiation in yeast S. cerevisiae.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Impairment of ribosomes and DNA biosynthesis confers resistance to Inhibition of sphingolipid biosynthesis.Molecular genetics and genomics : MGG · 2026Article
- Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function.International journal of molecular sciences · 2023Review
- Cryo-EM study of an archaeal 30S initiation complex gives insights into evolution of translation initiation.Communications biology · 2020Article
- Network theory of the bacterial ribosome.PloS one · 2020Article
- Recent Advances in Archaeal Translation Initiation.Frontiers in microbiology · 2020Review
- Article
- Role of the uS9/yS16 C-terminal tail in translation initiation and elongation in Saccharomyces cerevisiae.Nucleic acids research · 2019Article
- Non-canonical role of cancer-associated mutant SEC23B in the ribosome biogenesis pathway.Human molecular genetics · 2018Article
- Article
- Eukaryote-specific extensions in ribosomal proteins of the small subunit: Structure and function.Translation (Austin, Tex.)Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Conserved ribosomal proteins frequently harbor additional segments in eukaryotes not found in bacteria, which could facilitate eukaryotic-specific reactions in the initiation phase of protein synthesis. Here we provide evidence showing that truncation of the N-terminal domain (NTD) of yeast Rps5 (absent in bacterial ortholog S7) impairs translation initiation, cell growth and induction of GCN4 mRNA translation in a manner suggesting incomplete assembly of 48S preinitiation complexes (PICs) at upstream AUG codons in GCN4 mRNA. Rps5 mutations evoke accumulation of factors on native 40S subunits normally released on conversion of 48S PICs to 80S initiation complexes (ICs) and this abnormality and related phenotypes are mitigated by the SUI5 variant of eIF5. Remarkably, similar effects are observed by substitution of Lys45 in the Rps5-NTD, involved in contact with Rps16, and by eliminating the last two residues of the C-terminal tail (CTT) of Rps16, believed to contact initiator tRNA base-paired to AUG in the P site. We propose that Rps5-NTD-Rps16-NTD interaction modulates Rps16-CTT association with Met-tRNAi (Met) to promote a functional 48S PIC.
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