ArticleProceedings of the National Academy of Sciences of the United States of America2007
Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 82 citations in OpenAlex.
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- Structural and mechanistic basis for the heterotetrameric benzaldehyde synthase from petunia.Science advances · 2026Article
- Comparative Physiological and Transcriptomics Profiling Provides Integrated Insight into Melatonin Mediated Salt and Copper Stress Tolerance inPlants (Basel, Switzerland) · 2024Article
- TheFrontiers in plant science · 2024Article
- NTRC regulates CP12 to activate Calvin-Benson cycle during cold acclimation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Glyceraldehyde-3-phosphate dehydrogenase subunits A and B are essential to maintain photosynthetic efficiency.Plant physiology · 2023Article
- Reciprocity between a retrograde signal and a putative metalloprotease reconfigures plastidial metabolic and structural states.Science advances · 2022Article
- Proteomics approach to investigating osmotic stress effects on pistachio.Frontiers in plant science · 2022Article
- Proteomic Analysis of Rice Subjected to Low Light Stress and Overexpression of OsGAPB Increases the Stress Tolerance.Rice (New York, N.Y.) · 2020Article
- Photosynthetic Phosphoribulokinase Structures: Enzymatic Mechanisms and the Redox Regulation of the Calvin-Benson-Bassham Cycle.The Plant cell · 2020Article
- Redox-Mediated Post-Translational Modifications of Proteolytic Enzymes and Their Role in Protease Functioning.Biomolecules · 2020Review
- Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Genome-wide identification, characterization, interaction network and expression profile ofPeerJ · 2019Article
- Phosphoglycerate Kinases Are Co-Regulated to Adjust Metabolism and to Optimize Growth.Plant physiology · 2018Article
- Fairy "tails": flexibility and function of intrinsically disordered extensions in the photosynthetic world.Frontiers in molecular biosciences · 2015Review
- Thioredoxin-dependent redox regulation of chloroplastic phosphoglycerate kinase from Chlamydomonas reinhardtii.The Journal of biological chemistry · 2014Article
- Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Chemical reviews · 2014Review
- The yeast autophagy protease Atg4 is regulated by thioredoxin.Autophagy · 2014Article
- Redox regulation of the Calvin-Benson cycle: something old, something new.Frontiers in plant science · 2013Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chloroplast glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a light-regulated, NAD(P)H-dependent enzyme involved in plant photosynthetic carbon reduction. Unlike lower photosynthetic organisms, which only contain A(4)-GAPDH, the major GAPDH isoform of land plants is made up of A and B subunits, the latter containing a C-terminal extension (CTE) with fundamental regulatory functions. Light-activation of AB-GAPDH depends on the redox state of a pair of cysteines of the CTE, which can form a disulfide bond under control of thioredoxin f, leading to specific inhibition of the NADPH-dependent activity. The tridimensional structure of A(2)B(2)-GAPDH from spinach chloroplasts, crystallized in the oxidized state, shows that each disulfide-containing CTE is docked into a deep cleft between a pair of A and B subunits. The structure of the CTE was derived from crystallographic data and computational modeling and confirmed by site-specific mutagenesis. Structural analysis of oxidized A(2)B(2)-GAPDH and chimeric mutant [A+CTE](4)-GAPDH revealed that Arg-77, which is essential for coenzyme specificity and high NADPH-dependent activity, fails to interact with NADP in these kinetically inhibited GAPDH tetramers and is attracted instead by negative residues of oxidized CTE. Other subtle changes in catalytic domains and overall conformation of the tetramers were noticed in oxidized A(2)B(2)-GAPDH and [A+CTE](4)-GAPDH, compared with fully active A(4)-GAPDH. The CTE is envisioned as a redox-sensitive regulatory domain that can force AB-GAPDH into a kinetically inhibited conformation under oxidizing conditions, which also occur during dark inactivation of the enzyme in vivo.
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