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Updated: Feb 5, 2026

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
Published on: January 6, 2015
Argininosuccinate lyase from Escherichia coli as a novel DNA-binding protein
Jiwoun Park1, Jimin Min2, Jaeho Jeong1
1BioMedical Sciences Graduate Program, Chonnam National University, Gwangju, 61186, Republic of Korea.
Abstract:
Metabolic enzymes are increasingly recognized to perform functions beyond their canonical roles. Here, we report that Escherichia coli argininosuccinate lyase (ArgH), a central enzyme in arginine biosynthesis, directly binds duplex DNA in vitro. This study was prompted by reproducible observations of a nucleic acid-like component while isolating ArgH by anion-exchange chromatography. To characterize ArgH-DNA interactions, six duplex DNAs were selected based on structure-guided docking simulations (PADA1 and HDOCK), and their dissociation constants (KD) were determined by fluorescence spectroscopy. The KD values ranged from 60 to 200 nM, suggesting that the duplex DNAs interacted with ArgH strongly. These observations suggested ArgH as a previously unrecognized DNA-binding protein and provided a quantitative basis for exploring additional roles of this metabolic enzyme in nucleic acid-associated cellular processes.
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