ArticleThe Plant cell2007
Formation of DEG5 and DEG8 complexes and their involvement in the degradation of photodamaged photosystem II reaction center D1 protein in Arabidopsis.
Article in The Plant cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 95 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
95 citing papers in PubMed, 205 citations in OpenAlex.
- Chloroplast Protein Degradation Pathways During Leaf Senescence: Coordination and Roles in Nitrogen Remobilization.Plants (Basel, Switzerland) · 2026Review
- The GreenCut protein TEF6 maintains photosystem II homeostasis under high light by stabilizing FtsH accumulation in Chlamydomonas reinhardtii.Plant communications · 2026Article
- Conserved DNA architect couples chloroplast development to cell cycle in developing cotyledons.Nature plants · 2026Article
- What are grana in chloroplasts of vascular plants good for?Annals of botany · 2026Review
- Four guidelines to identify bona fide protease-substrate pairs.Journal of experimental botany · 2025Review
- Structure, regulation and assembly of the photosynthetic electron transport chain.Nature reviews. Molecular cell biology · 2025Review
- Characterization of Arabidopsis thaliana thylakoid lumen 7.6 protein functions in photosystem II assembly.Communications biology · 2025Article
- The thylakoid lumen Deg1 protease affects non-photochemical quenching via the levels of violaxanthin de-epoxidase and PsbS.The Plant journal : for cell and molecular biology · 2025Article
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Assembly and Repair of Photosystem II inPlants (Basel, Switzerland) · 2024Review
- The chromosome-scale genome and population genomics reveal the adaptative evolution ofHorticulture research · 2024Article
- Chloroplast gene expression: Recent advances and perspectives.Plant communications · 2023Review
- A large deletion conferring pale green leaves of maize.BMC plant biology · 2023Article
- Silencing of PepperInternational journal of molecular sciences · 2023Article
- The thylakoid membrane protein NTA1 is an assembly factor of the cytochrome bPlant communications · 2023Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- Physiological and transcriptomic analyses provide insight into thermotolerance in desert plant Zygophyllum xanthoxylum.BMC plant biology · 2023Article
- Downregulated expression ofPhotosynthetica · 2023Article
- Effects of abiotic stress on photosystem II proteins.Photosynthetica · 2023Review
- Chloroplasts Protein Quality Control and Turnover: A Multitude of Mechanisms.International journal of molecular sciences · 2022Review
35 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issuedCORRECTION.2018
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The widely distributed DEGP proteases play important roles in the degradation of damaged and misfolded proteins. Arabidopsis thaliana contains 16 DEGP-like proteases, four of which are located in the chloroplast. Here, we show that DEG5 and DEG8 form a hexamer in the thylakoid lumen and that recombinant DEG8 is proteolytically active toward both a model substrate (beta-casein) and photodamaged D1 protein of photosystem II (PSII), producing 16-kD N-terminal and 18-kD C-terminal fragments. Inactivation of DEG5 and DEG8 resulted in increased sensitivity to photoinhibition. Turnover of newly synthesized D1 protein in the deg5 deg8 double mutant was impaired, and the degradation of D1 in the presence of the chloroplast protein synthesis inhibitor lincomycin under high-light treatment was slowed in the mutants. Thus, DEG5 and DEG8 are important for efficient turnover of the D1 protein and for protection against photoinhibition in vivo. The deg5 deg8 double mutant showed increased photosensitivity and reduced rates of D1 degradation compared with single mutants of deg5 and deg8. A 16-kD N-terminal degradation fragment of the D1 protein was detected in wild-type plants but not in the deg5 deg8 mutant following in vivo photoinhibition. Therefore, our results suggest that DEG5 and DEG8 have a synergistic function in the primary cleavage of the CD loop of the PSII reaction center protein D1.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.