ArticleThe Plant cell2011
Subunit stoichiometry, evolution, and functional implications of an asymmetric plant plastid ClpP/R protease complex in Arabidopsis.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 78 citations in OpenAlex.
- Uncovering the role of the PPR protein PHOTOSYSTEM ONE BIOGENESIS FACTOR6 in splicing chloroplast group II introns.Journal of integrative plant biology · 2026Article
- Chloroplast Protein Degradation Pathways During Leaf Senescence: Coordination and Roles in Nitrogen Remobilization.Plants (Basel, Switzerland) · 2026Review
- The role of cytonuclear interactions to plant adaptation across aProceedings. Biological sciences · 2025Article
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- A chaperonin complex regulates organelle proteostasis in malaria parasites.PLoS pathogens · 2025Article
- Organellar transcripts dominate the cellular mRNA pool across plants of varying ploidy levels.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Gene duplication and rate variation in the evolution of plastid ACCase and Clp genes in angiosperms.Molecular phylogenetics and evolution · 2022Article
- The cryo-EM structure of the chloroplast ClpP complex.Nature plants · 2021Article
- The Welwitschia genome reveals a unique biology underpinning extreme longevity in deserts.Nature communications · 2021Article
- OsNBL1, a Multi-Organelle Localized Protein, Plays Essential Roles in Rice Senescence, Disease Resistance, and Salt Tolerance.Rice (New York, N.Y.) · 2021Article
- The Intron Retention VariantFrontiers in plant science · 2021Article
- Autocatalytic Processing and Substrate Specificity of Arabidopsis Chloroplast Glutamyl Peptidase.Plant physiology · 2020Article
- Role of ClpP in the Biogenesis and Degradation of RuBisCO and ATP Synthase inPlants (Basel, Switzerland) · 2019Article
- Consequences of the loss of catalytic triads in chloroplast CLPPR protease core complexes in vivo.Plant direct · 2018Article
- Temporal Proteomics of Inducible RNAi Lines of Clp Protease Subunits Identifies Putative Protease Substrates.Plant physiology · 2018Article
- Generation and characterization of a collection of knock-down lines for the chloroplast Clp protease complex in tobacco.Journal of experimental botany · 2017Article
- Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments.Plant physiology · 2016Review
- Determination of the Stoichiometry of the Complete Bacterial Type III Secretion Needle Complex Using a Combined Quantitative Proteomic Approach.Molecular & cellular proteomics : MCP · 2016Article
- Protein Phosphorylation and Redox Modification in Stomatal Guard Cells.Frontiers in physiology · 2016Review
- Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Nature reviews. Microbiology · 2016Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The caseinolytic protease (Clp) protease system has been expanded in plant plastids compared with its prokaryotic progenitors. The plastid Clp core protease consists of five different proteolytic ClpP proteins and four different noncatalytic ClpR proteins, with each present in one or more copies and organized in two heptameric rings. We determined the exact subunit composition and stoichiometry for the intact core and each ring. The chloroplast ClpP/R protease was affinity purified from clpr4 and clpp3 Arabidopsis thaliana null mutants complemented with C-terminal StrepII-tagged versions of CLPR4 and CLPP3, respectively. The subunit stoichiometry was determined by mass spectrometry-based absolute quantification using stable isotope-labeled proteotypic peptides generated from a synthetic gene. One heptameric ring contained ClpP3,4,5,6 in a 1:2:3:1 ratio. The other ring contained ClpP1 and ClpR1,2,3,4 in a 3:1:1:1:1 ratio, resulting in only three catalytic sites. These ClpP1/R1-4 proteins are most closely related to the two subunits of the cyanobacterial P3/R complex and the identical P:R ratio suggests conserved adaptation. Furthermore, the plant-specific C-terminal extensions of the ClpP/R subunits were not proteolytically removed upon assembly, suggesting a regulatory role in Clp chaperone interaction. These results will now allow testing ClpP/R structure-function relationships using rationale design. The quantification workflow we have designed is applicable to other protein complexes.
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