학술논문

Distinct paths for basic amino acid export in Escherichia coli: YbjE (LysO) mediates export of l-lysine
Document Type
Report
Author abstract
Source
Journal of Bacteriology. June, 2015, Vol. 197 Issue 11-12, p2036, 12 p.
Subject
Membrane proteins -- Analysis
Genetic transcription -- Research
Escherichia coli -- Genetic aspects
Escherichia coli -- Physiological aspects
Escherichia coli -- Research
Biological sciences
Language
English
ISSN
0021-9193
Abstract
In Escherichia coli, argO encodes an exporter for l-arginine (Arg) and its toxic analogue canavanine (CAN), and its transcriptional activation and repression, by Arg and l-lysine (Lys), respectively, are mediated by the regulator ArgP. Accordingly argO and argP mutants are CAN supersensitive (CANss). We report the identification of ybjE as a gene encoding a predicted inner membrane protein that mediates export of Lys, and our results confirm the previous identification with a different approach of YbjE as a Lys exporter, reported by Ueda and coworkers (T. Ueda, Y. Nakai, Y. Gunji, R. Takikawa, and Y. Joe, U.S. patents 7,629,142 B2 [December 2009] and 8,383,363 B1 [February 2013] and European patent 1,664,318 B1 [September 2009]). ybjE was isolated as a multicopy suppressor of the CANss phenotype of a strain lacking ArgO. The absence of YbjE did not confer a CANss phenotype but instead conferred hypersensitivity to the lysine antimetabolite thialysine and led to growth inhibition by the dipeptide lysylalanine, which is associated with elevated cellular Lys content. YbjE overproduction resulted in Lys excretion and syntrophic cross-feeding of a Lys auxotroph. Constitutive overexpression of argO promoted Lys cross-feeding that is indicative of a latent Lys export potential of ArgO. Arg modestly repressed ybjE transcription in an ArgR-dependent manner, and ArgR displayed Arg-sensitive binding to the ybjE promoter region in vitro. Our studies suggest that the reciprocal repression of argO and ybjE, respectively, by Lys and Arg confers the specificity for basic amino acid export by distinct paths and that such cross-repression contributes to maintenance of cytoplasmic Arg/Lys balance. We propose that YbjE be redesignated LysO.