ArticleThe Plant cell2015
Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts.
Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 46 citations in OpenAlex.
- High-dimensional CRISPR-SERS interactomics tracks the topological evolution of plant viral pathogenesis and therapeutic response.Chemical science · 2026Article
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis.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
- 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
- A Bivariate Mapping Model Identifies Major Covariation QTLs for Biomass Allocation Between Leaf and Stem Growth ofFrontiers in genetics · 2021Article
- Autocatalytic Processing and Substrate Specificity of Arabidopsis Chloroplast Glutamyl Peptidase.Plant physiology · 2020Article
- Protective Roles of Cytosolic and Plastidal Proteasomes on Abiotic Stress and Pathogen Invasion.Plants (Basel, Switzerland) · 2020Review
- Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.Scientific reports · 2019Article
- Co-suppression of NbClpC1 and NbClpC2 alters plant morphology with changed hormone levels in Nicotiana benthamiana.Plant cell reports · 2019Article
- Targeted Control of Chloroplast Quality to Improve Plant Acclimation: From Protein Import to Degradation.Frontiers in plant science · 2019Review
- 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
- Affinity purification with metabolomic and proteomic analysis unravels diverse roles of nucleoside diphosphate kinases.Journal of experimental botany · 2017Article
- Generation and characterization of a collection of knock-down lines for the chloroplast Clp protease complex in tobacco.Journal of experimental botany · 2017Article
- Crystal structures reveal N-terminal Domain of Arabidopsis thaliana ClpD to be highly divergent from that of ClpC1.Scientific reports · 2017Article
- Both Hsp70 chaperone and Clp protease plastidial systems are required for protection against oxidative stress.Plant signaling & behavior · 2017Article
- Two Isoforms of Clp Peptidase in Pseudomonas aeruginosa Control Distinct Aspects of Cellular Physiology.Journal of bacteriology · 2017Article
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
Plastid ClpT1 and ClpT2 are plant-specific proteins that associate with the ClpPR protease. However, their physiological significance and structures are not understood. Arabidopsis thaliana loss-of-function single clpt1 and clpt2 mutants showed no visible phenotypes, whereas clpt1 clpt2 double mutants showed delayed development, reduced plant growth, and virescent, serrated leaves but were viable and produced seed. The clpt1 and clpt1 clpt2 mutants showed partial destabilization of the ClpPR complex, whereas clpt2 null mutants showed only marginal destabilization. Comparative proteomics of clpt1 clpt2 plants showed a proteostasis phenotype similar to viable mutants in ClpPR core subunits, indicating reduced Clp protease capacity. In vivo and in vitro assays showed that ClpT1 and ClpT2 can independently interact with the single ClpP ring and ClpPR core, but not with the single ClpR ring. We determined ClpT1 and ClpT2 structures (2.4- and 2.0-Å resolution) and detailed the similarities to the N-domains of bacterial ClpA/C chaperones. The ClpT structures suggested a conserved MYFF motif for interaction with the ClpPR core near the interface between the P- and R-rings. In vivo complementation showed that ClpT function and ClpPR core stabilization require the MYFF motif. Several models are presented that may explain how ClpT1,2 contribute to ClpPR protease activity.
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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.