ArticleCell stress & chaperones2001
The Hsp90 family of proteins in Arabidopsis thaliana.
Article in Cell stress & chaperones, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.
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135 citing papers in PubMed, 358 citations in OpenAlex.
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- Interplay of p23 with FKBP51 and their chaperone complex in regulating tau aggregation.Nature communications · 2025Article
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- Viral proteins resolve the virus-vector conundrum during hemipteran-mediated transmission by subverting salicylic acid signaling pathway.Nature communications · 2024Article
- Enhancing Coleoptile Length of Rice Seeds under Submergence throughPlants (Basel, Switzerland) · 2024Article
- Genome-wide identification of3 Biotech · 2024Article
- Genome-wide identification, classification and expression analysis of the heat shock transcription factor family in Garlic (Allium sativum L.).BMC plant biology · 2024Article
- Genome-Wide Analysis of the Oat (International journal of molecular sciences · 2024Article
- Article
- Spatiotemporal expression patterns of cytosolic AtHSP90-2 inPlant signaling & behavior · 2023Article
- HEAT SHOCK PROTEIN 90.6 interacts with carbon and nitrogen metabolism components during seed development.Plant physiology · 2023Article
- Physiological and transcriptomic analyses provide insight into thermotolerance in desert plant Zygophyllum xanthoxylum.BMC plant biology · 2023Article
- Identification of a pluripotency-inducing small compound, PLU, that induces callus formationFrontiers in plant science · 2023Article
- Genome-wide analysis of Hsp40 and Hsp70 gene family in four cotton species provides insights into their involvement in response toFrontiers in genetics · 2023Article
- Responses of the tree peony (Paeonia suffruticosa, Paeoniaceae) cultivar 'Yu Hong' to heat stress revealed by iTRAQ-based quantitative proteomics.Proteome science · 2022Article
75 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 90-kDa heat shock protein (Hsp90) is an essential molecular chaperone in eukaryotic cells, with key roles in the folding and activation of proteins involved in signal transduction and control of the cell cycle. A search for Hsp90 sequences in the Arabidopsis thaliana genome revealed that this family includes 7 members. The AtHsp90-1 through AtHsp90-4 proteins constitute the cytoplasmic subfamily, whereas the AtHsp90-5, AtHsp90-6, and AtHsp90-7 proteins are predicted to be within the plastidial, mitochondrial, and endoplasmic reticulum compartments, respectively. The deduced amino acid sequences of each of the cytoplasmic proteins contains the highly conserved C-terminal pentapeptide MEEVD. All of the AtHsp90 sequences include a conserved adenosine triphosphate-binding domain, whereas only the cytoplasmic and endoplasmic reticulum-resident sequences include an adjacent charged linker domain that is common in mammalian and yeast sequences. The occurrence of multiple AtHsp90 proteins in the cytoplasm and of family members in other subcellular compartments suggests a range of specific functions and target polypeptides.
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