ArticleJournal of bacteriology2004
Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- An extragenic fix for a broken enzyme.Microbiology (Reading, England) · 2026Article
- Article
- Harnessing prokaryotic amino acid transporters for metabolic engineering: mechanisms and biotechnological applications.Synthetic and systems biotechnology · 2026Review
- Bacteriophage-mediated cell lysis externalizes a metabolically valuable nutrient to broadly modulate bacterial communities.The ISME journal · 2026Article
- Novel Regulators of the flhDC Gene Encoding the Flagella Master Regulator in Escherichia Coli K-12.Current microbiology · 2025Article
- Molecular interplay between peptidoglycan integrity and outer membrane asymmetry in maintaining cell envelope homeostasis.Journal of bacteriology · 2025Article
- Plant amino acid analogues as antimicrobial agents.Amino acids · 2025Review
- Fundamentals and Exceptions of the LysR-type Transcriptional Regulators.ACS synthetic biology · 2024Review
- l-Alanine Exporter AlaE Functions as One of the d-Alanine Exporters inInternational journal of molecular sciences · 2023Article
- Metabolic engineering of Escherichia coli for efficient production of L-arginine.Applied microbiology and biotechnology · 2022Article
- Analysis of a Library ofAntibiotics (Basel, Switzerland) · 2022Article
- Review
- Topological analyses of the L-lysine exporter LysO reveal a critical role for a conserved pair of intramembrane solvent-exposed acidic residues.The Journal of biological chemistry · 2021Article
- High-yield production of L-serine through a novel identified exporter combined with synthetic pathway in Corynebacterium glutamicum.Microbial cell factories · 2020Article
- Cystine import is a valuable but risky process whose hazards Escherichia coli minimizes by inducing a cysteine exporter.Molecular microbiology · 2020Article
- L-Alanine Exporter, AlaE, ofInternational journal of molecular sciences · 2019Article
- Derailing the aspartate pathway of Mycobacterium tuberculosis to eradicate persistent infection.Nature communications · 2019Article
- The transcriptional regulator LysG (Rv1985c) of Mycobacterium tuberculosis activates lysE (Rv1986) in a lysine-dependent manner.PloS one · 2017Article
- The Topology of the l-Arginine Exporter ArgO Conforms to an Nin-Cout Configuration in Escherichia coli: Requirement for the Cytoplasmic N-Terminal Domain, Functional Helical Interactions, and an Aspartate Pair for ArgO Function.Journal of bacteriology · 2016Article
- Bacterial Cysteine-Inducible Cysteine Resistance Systems.Journal of bacteriology · 2016Article
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2 authors.
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Abstract
The anonymous open reading frame yggA of Escherichia coli was identified in this study as a gene that is under the transcriptional control of argP (previously called iciA), which encodes a LysR-type transcriptional regulator protein. Strains with null mutations in either yggA or argP were supersensitive to the arginine analog canavanine, and yggA-lac expression in vivo exhibited argP(+)-dependent induction by arginine. Lysine supplementation phenocopied the argP null mutation in that it virtually abolished yggA expression, even in the argP+ strain. The dipeptides arginylalanine and lysylalanine behaved much like arginine and lysine, respectively, to induce and to turn off yggA transcription. Dominant missense mutations in argP (argPd) that conferred canavanine resistance and rendered yggA-lac expression constitutive were obtained. The protein deduced to be encoded by yggA shares similarity with a basic amino acid exporter (LysE) of Corynebacterium glutamicum, and we obtained evidence for increased arginine efflux from E. coli strains with either the argPd mutation or multicopy yggA+. The null yggA mutation abolished the increased arginine efflux from the argPd strain. Our results suggest that yggA encodes an ArgP-regulated arginine exporter, and we have accordingly renamed it argO (for "arginine outward transport"). We propose that the physiological function of argO may be either to prevent the accumulation to toxic levels of canavanine (which is a plant-derived antimetabolite) or arginine or to maintain an appropriate balance between the intracellular lysine and arginine concentrations.
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