ArticleCell stress & chaperones2002
The eukaryote chaperonin CCT is a cold shock protein in Saccharomyces cerevisiae.
Article in Cell stress & chaperones, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 39 citations in OpenAlex.
- Comparative Population Transcriptomics Provide New Insight into the Evolutionary History and Adaptive Potential of World Ocean Krill.Molecular biology and evolution · 2023Article
- Integrated Analysis of DNA Methylome and Transcriptome Reveals Epigenetic Regulation of Cold Tolerance inInternational journal of molecular sciences · 2023Article
- The potential of cold-shock promoters for the expression of recombinant proteins in microbes and mammalian cells.Journal, genetic engineering & biotechnology · 2022Review
- The intrinsic chaperone network of Arabidopsis stem cells confers protection against proteotoxic stress.Aging cell · 2021Article
- Convergent Evolution and Structural Adaptation to the Deep Ocean in the Protein-Folding Chaperonin CCTα.Genome biology and evolution · 2020Article
- Unveiling Kiwifruit Metabolite and Protein Changes in the Course of Postharvest Cold Storage.Frontiers in plant science · 2019Article
- Autolysis of Pichia pastoris induced by cold.AMB Express · 2017Article
- Gpd1 Regulates the Activity of Tcp-1 and Heat Shock Response in Yeast Cells: Effect on Aggregation of Mutant Huntingtin.Molecular neurobiology · 2016Article
- Characterization of CCTα and evaluating its expression in the mud crab Scylla paramamosain when challenged by low temperatures alone and in combination with high and low salinity.Cell stress & chaperones · 2015Article
- Evolutionary genomics of Culex pipiens: global and local adaptations associated with climate, life-history traits and anthropogenic factors.Proceedings. Biological sciences · 2015Article
- Article
- Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Article
- Up-regulation of heat shock proteins is essential for cold survival during insect diapause.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems.The Biochemical journal · 2006Review
- Heat shock response of Archaeoglobus fulgidus.Journal of bacteriology · 2005Article
- Expression of mRNA for the t-complex polypeptide-1, a subunit of chaperonin CCT, is upregulated in association with increased cold hardiness in Delia antiqua.Cell stress & chaperones · 2005Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The eukaryotic Hsp60 cytoplasmic chaperonin CCT (chaperonin containing the T-complex polypeptide-1) is essential for growth in budding yeast, and mutations in individual CCT subunits have been shown to affect assembly of tubulin and actin. The present research focused mainly on the expression of the CCT subunits, CCTalpha and CCTbeta, in yeast (Saccharomyces cerevisiae). Previous studies showed that, unlike most other chaperones, CCT in yeast does not undergo induction following heat shock. In this study, messenger ribonucleic acid (mRNA) and protein levels of CCT subunits following exposure to low temperatures, were examined. The Northern blot analysis indicated a 3- to 4-fold increase in mRNA levels of CCTalpha and CCTbeta genes after cold shock at 4 degrees C. Interestingly, Western blot analysis showed that cold shock induces an increase in the CCTalpha protein, which is expressed at 10 degrees C, but not at 4 degrees C. Transfer of 4 degrees C cold-shocked cells to 10 degrees C induced a 5-fold increase in the CCTalpha protein level. By means of fluorescent immunostaining and confocal microscopy, we found CCTalpha to be localized in the cortex and the cell cytoplasm of S. cerevisiae. Localization of CCTalpha was not affected at low temperatures. Co-localization of CCT and filaments of actin and tubulin was not observed by microscopy. The induction pattern of the CCTalpha protein suggests that expression of the chaperonin may be primarily important during the recovery from low temperatures and the transition to growth at higher temperatures, as found for other Hsps during the recovery phase from heat shock.
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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.