ArticleThe Journal of biological chemistry2011
Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
- Uvr motifs regulate the chloroplast Clp chaperone-protease system.Trends in plant science · 2025Review
- Genome-wide identification and expression analysis of heat shock protein gene family in cassava.The plant genome · 2023Article
- Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.The Plant cell · 2020Article
- Biochemical characterization of ClpB3, a chloroplastic disaggregase from Arabidopsis thaliana.Plant molecular biology · 2020Article
- Protein Import Motors in Chloroplasts: On the Role of Chaperones.The Plant cell · 2020Article
- Impaired PSII proteostasis triggers a UPR-like response in the var2 mutant of Arabidopsis.Journal of experimental botany · 2019Article
- The integration of chloroplast protein targeting with plant developmental and stress responses.BMC biology · 2017Review
- Crystal structures reveal N-terminal Domain of Arabidopsis thaliana ClpD to be highly divergent from that of ClpC1.Scientific reports · 2017Article
- Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms.Frontiers in plant science · 2017Review
- Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments.Plant physiology · 2016Review
- Chloroplast Hsp93 Directly Binds to Transit Peptides at an Early Stage of the Preprotein Import Process.Plant physiology · 2016Article
- Analysis of Drought-Induced Proteomic and Metabolomic Changes in Barley (Hordeum vulgare L.) Leaves and Roots Unravels Some Aspects of Biochemical Mechanisms Involved in Drought Tolerance.Frontiers in plant science · 2016Article
- Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.Plant physiology · 2016Article
- Discovery of a Unique Clp Component, ClpF, in Chloroplasts: A Proposed Binary ClpF-ClpS1 Adaptor Complex Functions in Substrate Recognition and Delivery.The Plant cell · 2015Article
- Sequence Motifs in Transit Peptides Act as Independent Functional Units and Can Be Transferred to New Sequence Contexts.Plant physiology · 2015Article
- New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Journal of molecular biology · 2015Review
- Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones.BMC plant biology · 2014Article
- 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.The Journal of biological chemistry · 2014Article
- Recombinant protein expression in Escherichia coli: advances and challenges.Frontiers in microbiology · 2014Review
- ClpS1 is a conserved substrate selector for the chloroplast Clp protease system in Arabidopsis.The Plant cell · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HSP100 proteins are molecular chaperones involved in protein quality control. They assist in protein (un)folding, prevent aggregation, and are thought to participate in precursor translocation across membranes. Caseinolytic proteins ClpC and ClpD from plant chloroplasts belong to the HSP100 family. Their role has hitherto been investigated by means of physiological studies and reverse genetics. In the present work, we employed an in vitro approach to delve into the structural and functional characteristics of ClpC2 and ClpD from Arabidopsis thaliana (AtClpC2 and AtClpD). They were expressed in Escherichia coli and purified to near-homogeneity. The proteins were detected mainly as dimers in solution, and, upon addition of ATP, the formation of hexamers was observed. Both proteins exhibited basal ATPase activity (K(m), 1.42 mm, V(max), 0.62 nmol/(min × μg) for AtClpC2 and K(m) ∼19.80 mm, V(max) ∼0.19 nmol/(min × μg) for AtClpD). They were able to reactivate the activity of heat-denatured luciferase (∼40% for AtClpC2 and ∼20% for AtClpD). The Clp proteins tightly bound a fusion protein containing a model transit peptide. This interaction was detected by binding assays, where the chaperones were selectively trapped by the transit peptide-containing fusion, immobilized on glutathione-agarose beads. Association of HSP100 proteins to import complexes with a bound transit peptide-containing fusion was also observed in intact chloroplasts. The presented data are useful to understand protein quality control and protein import into chloroplasts in plants.
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