ArticleThe Journal of biological chemistry2009
Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 82 citations in OpenAlex.
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- Optimization of the Chemical Monoubiquitination System for Low-Solubility Protein: Achieving Balance Between Specificity and Yield.Current issues in molecular biology · 2026Article
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- Benzoic and salicylic acids inhibit β-substituted alanine synthase 4;1 in common bean.Plant physiology · 2025Article
- Cysteine synthase: multiple structures of a key enzyme in cysteine synthesis and a potential drug target for Chagas disease and leishmaniasis.Acta crystallographica. Section D, Structural biology · 2023Article
- Serine acetyltransferase from Neisseria gonorrhoeae; structural and biochemical basis of inhibition.The Biochemical journal · 2022Article
- Tuberomics: a molecular profiling for the adaption of edible fungi (Tuber magnatum Pico) to different natural environments.BMC genomics · 2020Article
- Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action.International journal of molecular sciences · 2019Article
- Impact of overexpression of cytosolic isoform of O-acetylserine sulfhydrylase on soybean nodulation and nodule metabolome.Scientific reports · 2018Article
- Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex.FEBS letters · 2017Article
- β-N-Oxalyl-l-α,β-diaminopropionic Acid (β-ODAP) Content in Lathyrus sativus: The Integration of Nitrogen and Sulfur Metabolism through β-Cyanoalanine Synthase.International journal of molecular sciences · 2017Review
- Moonlighting O-acetylserine sulfhydrylase: New functions for an old protein.Biochimica et biophysica acta · 2015Review
- Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ·LysW complex from Thermus thermophilus.The Journal of biological chemistry · 2015Article
- Characterization of the serine acetyltransferase gene family of Vitis vinifera uncovers differences in regulation of OAS synthesis in woody plants.Frontiers in plant science · 2015Article
- Affinity Purification of O-Acetylserine(thiol)lyase from Chlorella sorokiniana by Recombinant Proteins from Arabidopsis thaliana.Metabolites · 2014Article
- Structure of soybean serine acetyltransferase and formation of the cysteine regulatory complex as a molecular chaperone.The Journal of biological chemistry · 2013Article
- Nucleotide binding site communication in Arabidopsis thaliana adenosine 5'-phosphosulfate kinase.The Journal of biological chemistry · 2012Article
- Mitochondrial cysteine synthase complex regulates O-acetylserine biosynthesis in plants.The Journal of biological chemistry · 2012Article
- Structure of Leishmania major cysteine synthase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Structure of soybean β-cyanoalanine synthase and the molecular basis for cyanide detoxification in plants.The Plant cell · 2012Article
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Authors and funding
4 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Macromolecular assemblies play critical roles in regulating cellular functions. The cysteine synthase complex (CSC), which is formed by association of serine O-acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS), acts as a sensor and modulator of thiol metabolism by responding to changes in nutrient conditions. Here we examine the oligomerization and energetics of formation of the soybean CSC. Biophysical examination of the CSC by size exclusion chromatography and sedimentation ultracentrifugation indicates that this assembly (complex M(r) approximately 330,000) consists of a single SAT trimer (trimer M(r) approximately 110,000) and three OASS dimers (dimer M(r) approximately 70,000). Analysis of the SAT-OASS interaction by isothermal titration calorimetry reveals negative cooperativity with three distinct binding events during CSC formation with K(d) values of 0.3, 7.5, and 78 nm. The three binding events are also observed using surface plasmon resonance with comparable affinities. The stability of the CSC derives from rapid association and extremely slow dissociation of OASS with SAT and requires the C terminus of SAT for the interaction. Steady-state kinetic analysis shows that CSC formation enhances SAT activity and releases SAT from substrate inhibition and feedback inhibition by cysteine, the final product of the biosynthesis pathway. Cysteine inhibits SAT and the CSC with K(i) values of 2 and 70 microm, respectively. These results suggest a new model for the architecture of this regulatory complex and additional control mechanisms for biochemically controlling plant cysteine biosynthesis. Based on previous work and our results, we suggest that OASS acts as an enzyme chaperone of SAT in the CSC.
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