ArticleThe Journal of cell biology1996
The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 49 citations in OpenAlex.
- Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.PLoS biology · 2022Article
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- Proteome profiling and vector yield optimization in a recombinant adeno-associated virus-producing yeast model.MicrobiologyOpen · 2020Article
- Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones.International journal of molecular sciences · 2019Review
- The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast.The Journal of biological chemistry · 2018Article
- Studying Huntington's Disease in Yeast: From Mechanisms to Pharmacological Approaches.Frontiers in molecular neuroscience · 2018Review
- Molecular cloning and functional analysis of the drought tolerance gene MsHSP70 from alfalfa (Medicago sativa L.).Journal of plant research · 2017Article
- Cloning and expression analysis of HSP70 gene from mangrove plant Kandelia obovata under cold stress.Ecotoxicology (London, England) · 2015Article
- Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Characterization of a wheat HSP70 gene and its expression in response to stripe rust infection and abiotic stresses.Molecular biology reports · 2011Article
- A novel scoring approach for protein co-purification data reveals high interaction specificity.PLoS computational biology · 2009Article
- The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiae.Journal of virology · 2008Article
- SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae.Cell stress & chaperones · 2007Article
- Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.The EMBO journal · 2006Article
- The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae.BMC genomics · 2005Article
- Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family.Plant physiology · 2001Article
- RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.Molecular biology of the cell · 1998Article
- Folding of active beta-lactamase in the yeast cytoplasm before translocation into the endoplasmic reticulum.Molecular biology of the cell · 1998Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ssa1/2p, members of one of the yeast cytosolic hsp70 subfamilies, have been implicated in the translocation of secretory proteins into the lumen of the ER. The involvement of these hsp70s in translocation was tested directly by examining the effect of immunodepleting Ssa1/2p from yeast cytosol and subsequently testing the cytosol for its ability to support co- and post-translational translocation of prepro-alpha-factor. Depletion of Ssa1/2p had no effect on the efficiency of translocation in this in vitro assay. The system was used to examine the effect of the absence of Ssa1/2p on two other putative hsp70 functions: cotranslational folding of nascent luciferase and refolding of denatured luciferase. Depletion of Ssa1/2p had no effect on the ability of the yeast lysate to synthesize enzymatically active luciferase, but had a dramatic effect on the ability of the lysate to refold chemically denatured luciferase. These results demonstrate, for the first time, the refolding activity of Ssa1/2p in the context of the yeast cytosol, and define refolding activity as a chaperone function specific to Ssa1/2p, aprt from other cytosolic hsp70s. They also suggest that Ssa1/2p do not play a significant role in chaperoning the folding of nascent polypeptides. The implications of these findings for Ssa1/2p activity on their proposed role in the process of translocation are discussed.
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