ArticleMolecular biology of the cell2008
Ribosome-associated complex binds to ribosomes in close proximity of Rpl31 at the exit of the polypeptide tunnel in yeast.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 89 citations in OpenAlex.
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- Nascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1.Molecular cell · 2026Article
- Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026Article
- Circadian clock control of ribosome composition promotes rhythmic translation and termination fidelity.Cell reports · 2025Article
- The Involvement ofBiology · 2024Article
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- Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate.Nature communications · 2023Article
- Structural inventory of cotranslational protein folding by the eukaryotic RAC complex.Nature structural & molecular biology · 2023Article
- Ribosomal protein L31 (RPL31) inhibits the proliferation and migration of gastric cancer cells.Heliyon · 2023Article
- Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023Review
- Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation.Nucleic acids research · 2022Article
- Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.Nature communications · 2022Article
- Pan-cancer analysis reveals DDX21 as a potential biomarker for the prognosis of multiple tumor types.Frontiers in oncology · 2022Article
- A role for the ribosome-associated complex in activation of the IRE1 branch of UPR.Cell reports · 2021Article
- Prevalence of ExoY Activity inFrontiers in microbiology · 2021Article
- Cooperativity between the Ribosome-Associated Chaperone Ssb/RAC and the Ubiquitin Ligase Ltn1 in Ubiquitination of Nascent Polypeptides.International journal of molecular sciences · 2020Article
- The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb.Nature communications · 2020Article
- Chaperone Interactions at the Ribosome.Cold Spring Harbor perspectives in biology · 2019Review
- A dual role of the ribosome-bound chaperones RAC/Ssb in maintaining the fidelity of translation termination.Nucleic acids research · 2019Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome-associated complex (RAC) consists of the Hsp40 homolog Zuo1 and the Hsp70 homolog Ssz1. The chaperone participates in the biogenesis of newly synthesized polypeptides. Here we have identified yeast Rpl31, a component of the large ribosomal subunit, as a contact point of RAC at the polypeptide tunnel exit. Rpl31 is encoded by RPL31a and RPL31b, two closely related genes. Delta rpl31a Delta rpl31b displayed slow growth and sensitivity to low as well as high temperatures. In addition, Delta rpl31a Delta rpl31b was highly sensitive toward aminoglycoside antibiotics and suffered from defects in translational fidelity. With the exception of sensitivity at elevated temperature, the phenotype resembled yeast strains lacking one of the RAC subunits or Rpl39, another protein localized at the tunnel exit. Defects of Delta rpl31a Delta rpl31b Delta zuo1 did not exceed that of Delta rpl31a Delta rpl31b or Delta zuo1. However, the combined deletion of RPL31a, RPL31b, and RPL39 was lethal. Moreover, RPL39 was a multicopy suppressor, whereas overexpression of RAC failed to rescue growth defects of Delta rpl31a Delta rpl31b. The findings are consistent with a model in that Rpl31 and Rpl39 independently affect a common ribosome function, whereas Rpl31 and RAC are functionally interdependent. Rpl31, while not essential for binding of RAC to the ribosome, might be involved in proper function of the chaperone complex.
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