Molecular analysis of the Corynebacterium glutamicum gene involved in lysine uptake

Publisher Website
Google Scholar
Abstract
Two Corynebacterium glutamicum mutants defective in lysine uptake were identified by analysing mutants resistant to S‐(2‐amtnoethyl)‐cysteine (AEC). A 5.6kb genomic DNA fragment restoring AEC sensitivity and lysine uptake was isolated. A 4.2kb subfragment was sequenced and three open reading frames were identified. Subcloning and gene disruption experiments showed that only the first open reading frame, termed lysl, is involved in lysine uptake. Lysl consists of 501 amino acids with a Mr of 53600. The hydrophobicity profile suggests that the lysl gene product is an integral membrane protein with 13 transmembrane segments. The amino acid sequence of lysl displays strong homology to that of the arcD gene product of Pseudomonas aeruginosa, which is proposed to act as an arginine–ornithine antiporter. Investigation of the influence of the lysl gene on lysine secretion suggests the existence of a separate lysine efflux system in C. glutamicum.