YjeH Is a Novel Exporter of l-Methionine and Branched-Chain Amino Acids in Escherichia coli

Applied and Environmental Microbiology
Qian LiuTingyi Wen

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 modelin...Continue Reading

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Citations

Oct 19, 2016·Current Opinion in Microbiology·Christian Rückert
Dec 3, 2016·Nucleic Acids Research·Ingrid M KeselerPeter D Karp
Jan 17, 2019·Bioinformatics·Philipp Schneider, Steffen Klamt
Nov 16, 2016·Journal of Industrial Microbiology & Biotechnology·Hua LiGui Yang Shi
Oct 9, 2019·International Journal of Molecular Sciences·Satoshi KatsubeHiroshi Yoneyama
May 1, 2021·Applied Microbiology and Biotechnology·Nurul Amira Mohammad MohanyHarald Janovjak

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