ReviewFrontiers in molecular biosciences2017
The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.
Review in Frontiers in molecular biosciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed.
- Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction.Nature communications · 2026Article
- Review
- SyntheticmicroPublication biology · 2025Article
- Perspectives on improving photosynthesis to increase crop yield.The Plant cell · 2024Review
- Down-regulation of wheat Rubisco activase isoforms expression by virus-induced gene silencing.Plant direct · 2024Article
- Towards engineering a hybrid carboxysome.Photosynthesis research · 2023Article
- High-throughput identification of novel heat tolerance genes via genome-wide pooled mutant screens in the model green alga Chlamydomonas reinhardtii.Plant, cell & environment · 2023Article
- Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases.Journal of experimental botany · 2023Article
- Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.Frontiers in molecular biosciences · 2023Review
- Review
- An Insight of RuBisCO Evolution through a Multilevel Approach.Biomolecules · 2021Article
- High light and temperature reduce photosynthetic efficiency through different mechanisms in the CCommunications biology · 2021Article
- Rubisco activase requires residues in the large subunit N terminus to remodel inhibited plant Rubisco.The Journal of biological chemistry · 2020Article
- Functional reconstitution of a bacterial COeLife · 2020Article
- The dependency of red Rubisco on its cognate activase for enhancing plant photosynthesis and growth.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Photons to food: genetic improvement of cereal crop photosynthesis.Journal of experimental botany · 2020Article
- Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Catalytic Role of RuBisCO forFrontiers in bioengineering and biotechnology · 2020Article
- DABs are inorganic carbon pumps found throughout prokaryotic phyla.Nature microbiology · 2019Article
- Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gaseous carbon dioxide enters the biosphere almost exclusively via the active site of the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). This highly conserved catalyst has an almost universal propensity to non-productively interact with its substrate ribulose 1,5-bisphosphate, leading to the formation of dead-end inhibited complexes. In diverse autotrophic organisms this tendency has been counteracted by the recruitment of dedicated AAA+ (ATPases associated with various cellular activities) proteins that all use the energy of ATP hydrolysis to remodel inhibited Rubisco active sites leading to release of the inhibitor. Three evolutionarily distinct classes of these Rubisco activases (Rcas) have been discovered so far. Green and red-type Rca are mostly found in photosynthetic eukaryotes of the green and red plastid lineage respectively, whereas CbbQO is associated with chemoautotrophic bacteria. Ongoing mechanistic studies are elucidating how the various motors are utilizing both similar and contrasting strategies to ultimately perform their common function of cracking the inhibited Rubisco active site. The best studied mechanism utilized by red-type Rca appears to involve transient threading of the Rubisco large subunit C-terminal peptide, reminiscent of the action performed by Clp proteases. As well as providing a fascinating example of convergent molecular evolution, Rca proteins can be considered promising crop-improvement targets. Approaches aiming to replace Rubisco in plants with improved enzymes will need to ensure the presence of a compatible Rca protein. The thermolability of the Rca protein found in crop plants provides an opportunity to fortify photosynthesis against high temperature stress. Photosynthesis also appears to be limited by Rca when light conditions are fluctuating. Synthetic biology strategies aiming to enhance the autotrophic CO
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.