ArticleThe Journal of biological chemistry2014
Quantitative analysis of the chloroplast molecular chaperone ClpC/Hsp93 in Arabidopsis reveals new insights into its localization, interaction with the Clp proteolytic core, and functional importance.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 60 citations in OpenAlex.
- Chloroplast Protein Degradation Pathways During Leaf Senescence: Coordination and Roles in Nitrogen Remobilization.Plants (Basel, Switzerland) · 2026Review
- Correlated Evolutionary Rates Reveal Novel Components and Cross-Compartment Connectivity in Plant Proteostasis Systems.Genome biology and evolution · 2026Article
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- Targeting signals required for protein sorting to sub-chloroplast compartments.Plant cell reports · 2024Review
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- Chloroplasts Protein Quality Control and Turnover: A Multitude of Mechanisms.International journal of molecular sciences · 2022Review
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- Protein Import Motors in Chloroplasts: On the Role of Chaperones.The Plant cell · 2020Article
- Protein import into chloroplasts and its regulation by the ubiquitin-proteasome system.Biochemical Society transactions · 2020Review
- Co-Suppression ofPlants (Basel, Switzerland) · 2020Article
- A Ycf2-FtsHi Heteromeric AAA-ATPase Complex Is Required for Chloroplast Protein Import.The Plant cell · 2018Article
- Combinations of Small RNA, RNA, and Degradome Sequencing Uncovers the Expression Pattern of microRNA⁻mRNA Pairs Adapting to Drought Stress in Leaf and Root ofInternational journal of molecular sciences · 2018Article
- The caseinolytic protease complex component CLPC1 in Arabidopsis maintains proteome and RNA homeostasis in chloroplasts.BMC plant biology · 2018Article
- Molecular Topology of the Transit Peptide during Chloroplast Protein Import.The Plant cell · 2018Article
- Control of Retrograde Signaling by Rapid Turnover of GENOMES UNCOUPLED1.Plant physiology · 2018Article
- Chloroplast Signaling Gates Thermotolerance in Arabidopsis.Cell reports · 2018Article
- Temporal Proteomics of Inducible RNAi Lines of Clp Protease Subunits Identifies Putative Protease Substrates.Plant physiology · 2018Article
- The integration of chloroplast protein targeting with plant developmental and stress responses.BMC biology · 2017Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular chaperone ClpC/Hsp93 is essential for chloroplast function in vascular plants. ClpC has long been held to act both independently and as the regulatory partner for the ATP-dependent Clp protease, and yet this and many other important characteristics remain unclear. In this study, we reveal that of the two near-identical ClpC paralogs (ClpC1 and ClpC2) in Arabidopsis chloroplasts, along with the closely related ClpD, it is ClpC1 that is the most abundant throughout leaf maturation. An unexpectedly large proportion of both chloroplast ClpC proteins (30% of total ClpC content) associates to envelope membranes in addition to their stromal localization. The Clp proteolytic core is also bound to envelope membranes, the amount of which is sufficient to bind to all the similarly localized ClpC. The role of such an envelope membrane Clp protease remains unclear although it appears uninvolved in preprotein processing or Tic subunit protein turnover. Within the stroma, the amount of oligomeric ClpC protein is less than that of the Clp proteolytic core, suggesting most if not all stromal ClpC functions as part of the Clp protease; a proposal supported by the near abolition of Clp degradation activity in the clpC1 knock-out mutant. Overall, ClpC appears to function primarily within the Clp protease, as the principle stromal protease responsible for maintaining homeostasis, and also on the envelope membrane where it possibly confers a novel protein quality control mechanism for chloroplast preprotein import.
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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.