ArticleMolecular biology of the cell1998
Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 83 citations in OpenAlex.
- Characterization of the interaction between the Sec61 translocon complex and ppαF using optical tweezers.Protein science : a publication of the Protein Society · 2024Article
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- Non-homologous End Joining-Mediated Insertional Mutagenesis Reveals a Novel Target for Enhancing Fatty Alcohols Production inFrontiers in microbiology · 2022Article
- Metalloporphyrin Pd(T4) Exhibits Oncolytic Activity and Cumulative Effects with 5-ALA Photodynamic Treatment against C918 Cells.International journal of molecular sciences · 2020Article
- Competition in the chaperone-client network subordinates cell-cycle entry to growth and stress.Life science alliance · 2019Article
- Synthesis and evaluation of esterified Hsp70 agonists in cellular models of protein aggregation and folding.Bioorganic & medicinal chemistry · 2019Article
- Mechanical properties of BiP protein determined by nano-rheology.Protein science : a publication of the Protein Society · 2018Article
- Iron affects Ire1 clustering propensity and the amplitude of endoplasmic reticulum stress signaling.Journal of cell science · 2017Article
- Single molecule force spectroscopy reveals the effect of BiP chaperone on protein folding.Protein science : a publication of the Protein Society · 2017Article
- Growth Rate as a Direct Regulator of the Start Network to Set Cell Size.Frontiers in cell and developmental biology · 2017Review
- A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.Journal of molecular biology · 2016Article
- Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis.The Journal of biological chemistry · 2014Article
- Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.PLoS genetics · 2014Article
- Article
- Analysis of ER resident proteins in Saccharomyces cerevisiae: implementation of H/KDEL retrieval sequences.Traffic (Copenhagen, Denmark) · 2013Article
- Chaperone stress 70 protein (STCH) binds and regulates two acid/base transporters NBCe1-B and NHE1.The Journal of biological chemistry · 2013Article
- The complex evolutionary dynamics of Hsp70s: a genomic and functional perspective.Genome biology and evolution · 2013Article
- The Candida albicans Kar2 protein is essential and functions during the translocation of proteins into the endoplasmic reticulum.Current genetics · 2011Article
- The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro.Cell stress & chaperones · 2010Article
- J domain co-chaperone specificity defines the role of BiP during protein translocation.The Journal of biological chemistry · 2010Article
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6 authors at 2 institutions in 1 country.
Funding
Abstract
The posttranslational translocation of proteins across the endoplasmic reticulum (ER) membrane in yeast requires ATP hydrolysis and the action of hsc70s (DnaK homologues) and DnaJ homologues in both the cytosol and ER lumen. Although the cytosolic hsc70 (Ssa1p) and the ER lumenal hsc70 (BiP) are homologous, they cannot substitute for one another, possibly because they interact with specific DnaJ homologues on each side of the ER membrane. To investigate this possibility, we purified Ssa1p, BiP, Ydj1p (a cytosolic DnaJ homologue), and a GST-63Jp fusion protein containing the lumenal DnaJ region of Sec63p. We observed that BiP, but not Ssa1p, is able to associate with GST-63Jp and that Ydj1p stimulates the ATPase activity of Ssa1p up to 10-fold but increases the ATPase activity of BiP by <2-fold. In addition, Ydj1p and ATP trigger the release of an unfolded polypeptide from Ssa1p but not from BiP. To understand further how BiP drives protein translocation, we purified four dominant lethal mutants of BiP. We discovered that each mutant is defective for ATP hydrolysis, fails to undergo an ATP-dependent conformational change, and cannot interact with GST-63Jp. Measurements of protein translocation into reconstituted proteoliposomes indicate that the mutants inhibit translocation even in the presence of wild-type BiP. We conclude that a conformation- and ATP-dependent interaction of BiP with the J domain of Sec63p is essential for protein translocation and that the specificity of hsc70 action is dictated by their DnaJ partners.
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