ArticleThe Journal of cell biology1996
The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA.
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 27 papers.
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Who cites it
27 citing papers in PubMed, 78 citations in OpenAlex.
- Mapping mitonuclear epistasis using a novel recombinant yeast population.PLoS genetics · 2023Article
- Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.Frontiers in molecular biosciences · 2022Review
- Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis.International journal of molecular sciences · 2020Article
- Heat shock protein 70 (HmHsp70) from Hypsizygus marmoreus confers thermotolerance to tobacco.AMB Express · 2020Article
- Redox Aspects of Chaperones in Cardiac Function.Frontiers in physiology · 2018Review
- Mitochondrial Cochaperone Mge1 Is Involved in Regulating Susceptibility to Fluconazole inmBio · 2017Article
- Precise genome-wide base editing by the CRISPR Nickase system in yeast.Scientific reports · 2017Article
- Article
- The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.Molecular biology of the cell · 2013Article
- Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp70 chaperone Ssc1.The Journal of biological chemistry · 2010Article
- Posttranslational regulation of the scaffold for Fe-S cluster biogenesis, Isu.Molecular biology of the cell · 2008Article
- Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins.The EMBO journal · 2006Article
- Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.The EMBO journal · 2005Article
- The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria.The EMBO journal · 2002Article
- Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.Molecular biology of the cell · 2002Article
- Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis.Molecular and cellular biology · 2000Article
- Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast.Microbiology and molecular biology reviews : MMBR · 2000Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
SSH1, a newly identified member of the heat shock protein (hsp70) multigene family of the budding yeast Saccharomyces cerevisiae, encodes a protein localized to the mitochondrial matrix. Deletion of the SSH1 gene results in extremely slow growth at 23 degrees C or 30 degrees C, but nearly wild-type growth at 37 degrees C. The matrix of the mitochondria contains another hsp70, Ssc1, which is essential for growth and required for translocation of proteins into mitochondria. Unlike SSC1 mutants, an SSH1 mutant showed no detectable defects in import of several proteins from the cytosol to the matrix compared to wild type. Increased expression of Ssc1 partially suppressed the cold-sensitive growth defect of the SSH1 mutant, suggesting that when present in increased amounts, Ssc1 can at least partially carry out the normal functions of Ssh1. Spontaneous suppressors of the cold-sensitive phenotype of an SSH1 null mutant were obtained at a high frequency at 23 degrees C, and were all found to be respiration deficient. 15 of 16 suppressors that were analyzed lacked mitochondrial DNA, while the 16th had reduced amounts. We suggest that Ssh1 is required for normal mitochondrial DNA replication, and that disruption of this process in ssh1 cells results in a defect in mitochondrial function at low temperatures.
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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.