ArticleNature communications2016
Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interaction.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Nascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1.Molecular cell · 2026Article
- The cotranslational cycle of the ribosome-bound Hsp70 homolog Ssb.Nature communications · 2026Article
- Electrochemical detection of cardiovascular diseases and treatment platform based on microfluidic technology.Mikrochimica acta · 2025Review
- NAC and Zuotin/Hsp70 chaperone systems coexist at the ribosome tunnel exit in vivo.Nucleic acids research · 2024Article
- Chaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis.PLoS biology · 2024Article
- The ribosome-associated chaperone Zuo1 controls translation upon TORC1 inhibition.The EMBO journal · 2023Article
- Principles, challenges, and advances in ribosome profiling: from bulk to low-input and single-cell analysis.Advanced biotechnology · 2023Review
- Yeast Chaperone Hsp70-Ssb Modulates a Variety of Protein-Based Heritable Elements.International journal of molecular sciences · 2023Article
- Structural inventory of cotranslational protein folding by the eukaryotic RAC complex.Nature structural & molecular biology · 2023Article
- Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.Nature communications · 2022Article
- Pathway of Hsp70 interactions at the ribosome.Nature communications · 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
- Fhl1p protein, a positive transcription factor in Pichia pastoris, enhances the expression of recombinant proteins.Microbial cell factories · 2019Article
- Chaperone Interactions at the Ribosome.Cold Spring Harbor perspectives in biology · 2019Review
- Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT.Molecular cell · 2019Article
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- Enhancing co-translational folding of heterologous protein by deleting non-essential ribosomal proteins inBiotechnology for biofuels · 2019Article
- Heat-Shock Proteins MoSsb1, MoSsz1, and MoZuo1 Attenuate MoMkk1-Mediated Cell-Wall Integrity Signaling and Are Important for Growth and Pathogenicity of Magnaporthe oryzae.Molecular plant-microbe interactions : MPMI · 2018Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Hsp70 chaperones assist de novo folding of newly synthesized proteins in all cells. In yeast, the specialized Hsp70 Ssb directly binds to ribosomes. The structural basis and functional mode of recruitment of Ssb to ribosomes is not understood. Here, we present the molecular details underlying ribosome binding of Ssb in Saccharomyces cerevisiae. This interaction is multifaceted, involving the co-chaperone RAC and two specific regions within Ssb characterized by positive charges. The C-terminus of Ssb mediates the key contact and a second attachment point is provided by a KRR-motif in the substrate binding domain. Strikingly, ribosome binding of Ssb is not essential. Autonomous ribosome attachment becomes necessary if RAC is absent, suggesting a dual mode of Ssb recruitment to nascent chains. We propose, that the multilayered ribosomal interaction allows positioning of Ssb in an optimal orientation to the tunnel exit guaranteeing an efficient nascent polypeptide interaction.
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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.