Two Distinct Assembly States of the Cysteine Regulatory Complex of Salmonella typhimurium Are Regulated by Enzyme–Substrate Cognate Pairs

• Published in: Biochemistry (Easton) Vol. 56; no. 18; pp. 2385 - 2399
• Main Authors: Kaushik, Abhishek, Ekka, Mary Krishna, Kumaran, Sangaralingam
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 09.05.2017
• Subjects: Binding Sites; biosynthesis; calorimetry; Cloning, Molecular; cysteine; Cysteine - biosynthesis; Cysteine - chemistry; cysteine synthase; Cysteine Synthase - chemistry; Cysteine Synthase - genetics; Cysteine Synthase - metabolism; enzyme substrates; Escherichia coli - genetics; Escherichia coli - metabolism; gel chromatography; Gene Expression; Gene Expression Regulation, Bacterial; Kinetics; Molecular Dynamics Simulation; Protein Binding; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Structure, Secondary; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Salmonella Typhimurium; Salmonella typhimurium - enzymology; Salmonella typhimurium - genetics; serine O-acetyltransferase; Serine O-Acetyltransferase - chemistry; Serine O-Acetyltransferase - genetics; Serine O-Acetyltransferase - metabolism; Substrate Specificity; sulfates; sulfides; surface plasmon resonance; titration; ultracentrifugation

Serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS), which catalyze the last two steps of cysteine biosynthesis, interact and form the cysteine regulatory complex (CRC). The current model of Salmonella typhimurium predicts that CRC is composed of one [SAT]hexamer unit and two mole...