ArticlePlant molecular biology2020
Biochemical characterization of ClpB3, a chloroplastic disaggregase from Arabidopsis thaliana.
Article in Plant molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Changes in proteome and protein carbonylation in potato (Solanum tuberosum L.) under single and combined abiotic stresses.Scientific reports · 2025Article
- A Holistic Investigation of Arabidopsis Proteomes Altered in Chloroplast Biogenesis and Retrograde Signalling Identifies PsbO as a Key Regulator of Chloroplast Quality Control.Plant, cell & environment · 2025Article
- A Genome-Wide Characterization of Receptor-like Cytoplasmic Kinase IV Subfamily Members inPlants (Basel, Switzerland) · 2024Article
- Methyl viologen-induced changes in the Arabidopsis proteome implicate PATELLIN 4 in oxidative stress responses.Journal of experimental botany · 2024Article
- CLPB3 is required for the removal of chloroplast protein aggregates and thermotolerance in Chlamydomonas.Journal of experimental botany · 2023Article
- Mapping yield and yield-related traits using diverse common bean germplasm.Frontiers in genetics · 2023Article
- A proteostasis network safeguards the chloroplast proteome.Essays in biochemistry · 2022Review
- Recruitment of an ancient branching program to suppress carpel development in maize flowers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Physiological and Proteomic Responses of Contrasting Alfalfa (Frontiers in plant science · 2021Article
- Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis.The Journal of biological chemistryReview
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
key messageThe first biochemical characterization of a chloroplastic disaggregase is reported (Arabidopsis thaliana ClpB3). ClpB3 oligomerizes into active hexamers that resolubilize aggregated substrates using ATP and without the aid of partners. Disaggregases from the Hsp100/Clp family are a type of molecular chaperones involved in disassembling protein aggregates. Plant cells are uniquely endowed with ClpB proteins in the cytosol, mitochondria and chloroplasts. Chloroplastic ClpB proteins have been implicated in key processes like the unfolded protein response; however, they have not been studied in detail. In this study, we explored the biochemical properties of a chloroplastic ClpB disaggregase, in particular, ClpB3 from A. thaliana. ClpB3 was produced recombinantly in Escherichia coli and affinity-purified to near homogeneity. ClpB3 forms a hexameric complex in the presence of MgATP and displays intrinsic ATPase activity. We demonstrate that ClpB3 has ATPase activity in a wide range of pH and temperature values and is particularly resistant to heat. ClpB3 specifically targets unstructured polypeptides and mediates the reactivation of heat-denatured model substrates without the aid of the Hsp70 system. Overall, this work represents the first in-depth biochemical description of a ClpB protein from plants and strongly supports its role as the putative disaggregase chaperone in chloroplasts.
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