ArticlePlant physiology2018
Temporal Proteomics of Inducible RNAi Lines of Clp Protease Subunits Identifies Putative Protease Substrates.
Article in Plant physiology, 2018. 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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Who cites it
23 citing papers in PubMed, 46 citations in OpenAlex.
- Metabolite control of enzyme activity links stress to biosynthetic regulation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Chloroplast ATP synthase: From structure to engineering.The Plant cell · 2024Review
- MEP pathway products allosterically promote monomerization of deoxy-D-xylulose-5-phosphate synthase to feedback-regulate their supply.Plant communications · 2023Article
- Characterization of mutants deficient in N-terminal phosphorylation of the chloroplast ATP synthase subunit β.Plant physiology · 2023Article
- The roles of plant proteases and protease inhibitors in drought response: a review.Frontiers in plant science · 2023Review
- Emergence of Novel RNA-Editing Sites by Changes in the Binding Affinity of a Conserved PPR Protein.Molecular biology and evolution · 2022Article
- Proteolytic regulation of mitochondrial oxidative phosphorylation components in plants.Biochemical Society transactions · 2022Review
- Rapid sequence evolution is associated with genetic incompatibilities in the plastid Clp complex.Plant molecular biology · 2022Article
- Topology of the redox network during induction of photosynthesis as revealed by time-resolved proteomics in tobacco.Science advances · 2021Article
- Correction of frameshift mutations in the atpB gene by translational recoding in chloroplasts of Oenothera and tobacco.The Plant cell · 2021Article
- Proteostatic Regulation of MEP and Shikimate Pathways by Redox-Activated Photosynthesis Signaling in Plants Exposed to Small Fungal Volatiles.Frontiers in plant science · 2021Article
- Article
- A Multi-OMICs Approach Sheds Light on the Higher Yield Phenotype and Enhanced Abiotic Stress Tolerance in Tobacco Lines Expressing the CarrotFrontiers in plant science · 2021Article
- Conserved and Unique Roles of Chaperone-Dependent E3 Ubiquitin Ligase CHIP in Plants.Frontiers in plant science · 2021Review
- Plastome sequences of the subgenus Passiflora reveal highly divergent genes and specific evolutionary features.Plant molecular biology · 2020Article
- Mitochondrial CLPP2 Assists Coordination and Homeostasis of Respiratory Complexes.Plant physiology · 2020Article
- Protein Import Motors in Chloroplasts: On the Role of Chaperones.The Plant cell · 2020Article
- Uncovering the functional residues ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Establishment of a Heterologous RNA Editing Event in Chloroplasts.Plant physiology · 2019Article
- Co-suppression of NbClpC1 and NbClpC2 alters plant morphology with changed hormone levels in Nicotiana benthamiana.Plant cell reports · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Clp protease in the chloroplasts of plant cells is a large complex composed of at least 13 nucleus-encoded subunits and one plastid-encoded subunit, which are arranged in several ring-like structures. The proteolytic P-ring and the structurally similar R-ring form the core complex that contains the proteolytic chamber. Chaperones of the HSP100 family help with substrate unfolding, and additional accessory proteins are believed to assist with Clp complex assembly and/or to promote complex stability. Although the structure and function of the Clp protease have been studied in great detail in both bacteria and chloroplasts, the identification of bona fide protease substrates has been very challenging. Knockout mutants of genes for protease subunits are of limited value, due to their often pleiotropic phenotypes and the difficulties with distinguishing primary effects (i.e. overaccumulation of proteins that represent genuine protease substrates) from secondary effects (proteins overaccumulating for other reasons). Here, we have developed a new strategy for the identification of candidate substrates of plant proteases. By combining ethanol-inducible knockdown of protease subunits with time-resolved analysis of changes in the proteome, proteins that respond immediately to reduced protease activity can be identified. In this way, secondary effects are minimized and putative protease substrates can be identified. We have applied this strategy to the Clp protease complex of tobacco (
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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.