ArticleApplied and environmental microbiology2015
YjeH Is a Novel Exporter of l-Methionine and Branched-Chain Amino Acids in Escherichia coli.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 49 citations in OpenAlex.
- Article
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- Development of a lysine biosensor for the dynamic regulation of cadaverine biosynthesis in E. coli.Microbial cell factories · 2025Article
- Identification and Characterization of a Novel d-Branched-Chain Amino Acids Importer from Lactobacillus fermentum.Chembiochem : a European journal of chemical biology · 2025Article
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- Engineering of a Substrate Affinity Reduced S-Adenosyl-methionine Synthetase as a Novel Biosensor for Growth-Coupling Selection of L-Methionine Overproducers.Applied biochemistry and biotechnology · 2024Article
- Systemic intracellular analysis for balancing complex biosynthesis in a transcriptionally deregulated Escherichia coli l-Methionine producer.Microbial biotechnology · 2024Article
- Conversion of methionine biosynthesis in Escherichia coli from trans- to direct-sulfurylation enhances extracellular methionine levels.Microbial cell factories · 2023Article
- Multivariate modular metabolic engineering for enhanced L-methionine biosynthesis in Escherichia coli.Biotechnology for biofuels and bioproducts · 2023Article
- Thorough research and modification of one-carbon units cycle for improving L-methionine production in3 Biotech · 2023Article
- TheMicroorganisms · 2022Article
- Microbial methionine transporters and biotechnological applications.Applied microbiology and biotechnology · 2021Review
- 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
- Characterizing and ranking computed metabolic engineering strategies.Bioinformatics (Oxford, England) · 2019Article
- Metabolic engineering of3 Biotech · 2018Article
- The EcoCyc database: reflecting new knowledge about Escherichia coli K-12.Nucleic acids research · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Amino acid efflux transport systems have important physiological functions and play vital roles in the fermentative production of amino acids. However, no methionine exporter has yet been identified in Escherichia coli. In this study, we identified a novel amino acid exporter, YjeH, in E. coli. The yjeH overexpression strain exhibited high tolerance to the structural analogues of l-methionine and branched-chain amino acids, decreased intracellular amino acid levels, and enhanced export rates in the presence of a Met-Met, Leu-Leu, Ile-Ile, or Val-Val dipeptide, suggesting that YjeH functions as an exporter of l-methionine and the three branched-chain amino acids. The export of the four amino acids in the yjeH overexpression strain was competitively inhibited in relation to each other. The expression of yjeH was strongly induced by increasing cytoplasmic concentrations of substrate amino acids. Green fluorescent protein (GFP)-tagged YjeH was visualized by total internal reflection fluorescence microscopy to confirm the plasma membrane localization of YjeH. Phylogenetic analysis of transporters indicated that YjeH belongs to the amino acid efflux family of the amino acid/polyamine/organocation (APC) superfamily. Structural modeling revealed that YjeH has the typical "5 + 5" transmembrane α-helical segment (TMS) inverted-repeat fold of APC superfamily transporters, and its binding sites are strictly conserved. The enhanced capacity of l-methionine export by the overexpression of yjeH in an l-methionine-producing strain resulted in a 70% improvement in titer. This study supplements the transporter classification and provides a substantial basis for the application of the methionine exporter in metabolic engineering.
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