ArticleThe Plant cell2011
Assembly of the chloroplast ATP-dependent Clp protease in Arabidopsis is regulated by the ClpT accessory proteins.
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 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 67 citations in OpenAlex.
- Article
- Fine mapping and identification of causal alleles at the Ur-11 locus controlling rust resistance in common bean (Phaseolus vulgaris L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Silencing an ATP-Dependent Caseinolytic Protease Proteolytic Subunit Gene Enhances the Resistance of Rice toInternational journal of molecular sciences · 2024Article
- AmCBF1 activates the expression of GhClpR1 to mediate dark-green leaves in cotton (Gossypium hirsutum).Plant cell reports · 2024Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- 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
- Plastid caseinolytic protease OsClpR1 regulates chloroplast development and chloroplast RNA editing in rice.Rice (New York, N.Y.) · 2021Article
- OsNBL1, a Multi-Organelle Localized Protein, Plays Essential Roles in Rice Senescence, Disease Resistance, and Salt Tolerance.Rice (New York, N.Y.) · 2021Article
- Protective Roles of Cytosolic and Plastidal Proteasomes on Abiotic Stress and Pathogen Invasion.Plants (Basel, Switzerland) · 2020Review
- Functional switching of NPR1 between chloroplast and nucleus for adaptive response to salt stress.Scientific reports · 2020Article
- Co-suppression of NbClpC1 and NbClpC2 alters plant morphology with changed hormone levels in Nicotiana benthamiana.Plant cell reports · 2019Article
- Consequences of the loss of catalytic triads in chloroplast CLPPR protease core complexes in vivo.Plant direct · 2018Article
- Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments.Plant physiology · 2016Review
- Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.Plant physiology · 2016Article
- Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts.The Plant cell · 2015Article
- Structure and activation of a heteromeric protease complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones.BMC plant biology · 2014Article
- Conditional Depletion of the Chlamydomonas Chloroplast ClpP Protease Activates Nuclear Genes Involved in Autophagy and Plastid Protein Quality Control.The Plant cell · 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
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ATP-dependent caseinolytic protease (Clp) is an essential housekeeping enzyme in plant chloroplasts. It is by far the most complex of all known Clp proteases, with a proteolytic core consisting of multiple catalytic ClpP and noncatalytic ClpR subunits. It also includes a unique form of Clp protein of unknown function designated ClpT, two of which exist in the model species Arabidopsis thaliana. Inactivation of ClpT1 or ClpT2 significantly reduces the amount of Clp proteolytic core, whereas loss of both proves seedling lethal under autotrophic conditions. During assembly of the Clp proteolytic core, ClpT1 first binds to the P-ring (consisting of ClpP3-6 subunits) followed by ClpT2, and only then does the P-ring combine with the R-ring (ClpP1, ClpR1-4 subunits). Most of the ClpT proteins in chloroplasts exist in vivo as homodimers, which then apparently monomerize prior to association with the P-ring. Despite their relative abundance, however, the availability of both ClpT proteins is rate limiting for the core assembly, with the addition of recombinant ClpT1 and ClpT2 increasing core content up to fourfold. Overall, ClpT appears to regulate the assembly of the chloroplast Clp protease, revealing a new and sophisticated control mechanism on the activity of this vital protease in plants.
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