ArticleThe Journal of biological chemistry2017
Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- SRP orchestrates protein biogenesis beyond initial ER membrane targeting.Nature communications · 2026Article
- Transmembrane effector substrates of type IV secretion systems: mechanisms of secretion and insertion into host cell membranes.microLife · 2026Review
- The Absence of Sec72 Reshapes Yeast Cell Functions to Increase Protein Secretion.Research (Washington, D.C.) · 2026Article
- Multi-Omics Analysis Reveals Impacts of LincRNA Deletion on Yeast Protein Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A kalihinol analog disrupts apicoplast function and vesicular trafficking inScience (New York, N.Y.) · 2024Article
- TTC17 is an endoplasmic reticulum resident TPR-containing adaptor protein.The Journal of biological chemistry · 2023Article
- Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond.International journal of molecular sciences · 2023Review
- Comprehensive Analysis of Signal Peptides in Saccharomyces cerevisiae Reveals Features for Efficient Secretion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Exploration of the truncated cytosolic Hsp70 in plants - unveiling the diverse T1 lineage and the conserved T2 lineage.Frontiers in plant science · 2023Article
- Mechanisms of mitochondrial respiratory adaptation.Nature reviews. Molecular cell biology · 2022Review
- Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022Review
- Volleying plasma membrane proteins from birth to death: Role of J-domain proteins.Frontiers in molecular biosciences · 2022Review
- Emerging View on the Molecular Functions of Sec62 and Sec63 in Protein Translocation.International journal of molecular sciences · 2021Review
- Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation.International journal of molecular sciences · 2021Review
- The chaperone-binding activity of the mitochondrial surface receptor Tom70 protects the cytosol against mitoprotein-induced stress.Cell reports · 2021Article
- Architecture of the active post-translational Sec translocon.The EMBO journal · 2021Article
- Plastid chaperone HSP90C guides precursor proteins to the SEC translocase for thylakoid transport.Journal of experimental botany · 2020Article
- Overlapping function of Hrd1 and Ste24 in translocon quality control provides robust channel surveillance.The Journal of biological chemistry · 2020Article
- The selectivity filter of the mitochondrial protein import machinery.BMC biology · 2020Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The biosynthesis of many eukaryotic proteins requires accurate targeting to and translocation across the endoplasmic reticulum membrane. Post-translational protein translocation in yeast requires both the Sec61 translocation channel, and a complex of four additional proteins: Sec63, Sec62, Sec71, and Sec72. The structure and function of these proteins are largely unknown. This pathway also requires the cytosolic Hsp70 protein Ssa1, but whether Ssa1 associates with the translocation machinery to target protein substrates to the membrane is unclear. Here, we use a combined structural and biochemical approach to explore the role of Sec71-Sec72 subcomplex in post-translational protein translocation. To this end, we report a crystal structure of the Sec71-Sec72 complex, which revealed that Sec72 contains a tetratricopeptide repeat (TPR) domain that is anchored to the endoplasmic reticulum membrane by Sec71. We also determined the crystal structure of this TPR domain with a C-terminal peptide derived from Ssa1, which suggests how Sec72 interacts with full-length Ssa1. Surprisingly, Ssb1, a cytoplasmic Hsp70 that binds ribosome-associated nascent polypeptide chains, also binds to the TPR domain of Sec72, even though it lacks the TPR-binding C-terminal residues of Ssa1. We demonstrate that Ssb1 binds through its ATPase domain to the TPR domain, an interaction that leads to inhibition of nucleotide exchange. Taken together, our results suggest that translocation substrates can be recruited to the Sec71-Sec72 complex either post-translationally through Ssa1 or co-translationally through Ssb1.
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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.