ArticleProceedings of the National Academy of Sciences of the United States of America2013
An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 113 citations in OpenAlex.
- Right place, right time: movement of a fungal effector between subcellular compartments activates plant immune responses.Plant physiology · 2026Article
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- Functional Interaction Between Toc75 POTRA1 Domain and Tic22-III in the Intermembrane Space During Chloroplast Protein Import.Plant direct · 2026Article
- Beyond Folding: Expanding the Functional Landscape of Hsp90 Chaperone Machinery in Health and Disease.International journal of molecular sciences · 2025Review
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- PlantConnectome: A knowledge graph database encompassing >71,000 plant articles.The Plant cell · 2025Article
- Mapping of identity by descent reveals genes shaping morphology and biological traits in the cultivated lettuce varieties during the long-term crossbreeding.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Regulatory and retrograde signaling networks in the chlorophyll biosynthetic pathway.Journal of integrative plant biology · 2025Review
- LHP1 and INO80 cooperate with ethylene signaling for warm ambient temperature response by activating specific bivalent genes.Cell reports · 2024Article
- Plastid Molecular Chaperone HSP90C Interacts with the SecA1 Subunit of Sec Translocase for Thylakoid Protein Transport.Plants (Basel, Switzerland) · 2024Article
- Chloroplast import motor subunits FtsHi1 and FtsHi2 are located on opposite sides of the inner envelope membrane.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Cloning of an Albino Mutation ofInternational journal of molecular sciences · 2023Article
- Effects of Mycotoxin Fumagillin, Mevastatin, Radicicol, and Wortmannin on Photosynthesis ofPlants (Basel, Switzerland) · 2023Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- The journey of preproteins across the chloroplast membrane systems.Frontiers in physiology · 2023Review
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- Chloroplast protein import machinery and quality control.The FEBS journal · 2022Review
- Split-Ubiquitin Two-Hybrid Screen for Proteins Interacting with slToc159-1 and slToc159-2, Two Chloroplast Preprotein Import Receptors in Tomato (Plants (Basel, Switzerland) · 2022Article
- Regulation of Protein Transport Pathways by the Cytosolic Hsp90s.Biomolecules · 2022Review
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Chloroplast heat shock protein 90 (Hsp90C) represents a highly conserved subfamily of the Hsp90 family of molecular chaperones whose function has not been defined. We identified Hsp90C as a component that interacts with import intermediates of nuclear-encoded preproteins during posttranslational import into isolated chloroplasts. Hsp90C was specifically coprecipitated with a complex of protein import components, including Tic110, Tic40, Toc75, Tic22, and the stromal chaperones, Hsp93 and Hsp70. Radicicol, an inhibitor of Hsp90 ATPase activity, reversibly inhibited the import of a variety of preproteins during translocation across the inner envelope membrane, indicating that Hsp90C functions in membrane translocation into the organelle. Hsp90C is encoded by a single gene in Arabidopsis thaliana, and insertion mutations in the Hsp90C gene are embryo lethal, indicating an essential function for the chaperone in plant viability. On the basis of these results, we propose that Hsp90C functions within a chaperone complex in the chloroplast stroma to facilitate membrane translocation during protein import into the organelle.
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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.