Abstract
Corynebacterium glutamicum is widely used for amino acid production. In the present study, 543 genes showed a significant change in their mRNA expression levels in l-lysine-producing C. glutamicum ATCC21300 than that in the wild-type C. glutamicum ATCC13032. Among these 543 differentially expressed genes (DEGs), 28 genes were up- or downregulated. In addition, 454 DEGs were functionally enriched and categorized based on BLAST sequence homologies and gene ontology (GO) annotations using the Blast2GO software. Interestingly, NCgl0071 (bioB, encoding biotin synthase) was expressed at levels ~20-fold higher in the l-lysine-producing ATCC21300 strain than that in the wild-type ATCC13032 strain. Five other genes involved in biotin metabolism or transport—NCgl2515 (bioA, encoding adenosylmethionine-8-amino-7-oxononanoate aminotransferase), NCgl2516 (bioD, encoding dithiobiotin synthetase), NCgl1883, NCgl1884, and NCgl1885—were also expressed at significantly higher levels in the l-lysine-producing ATCC21300 strain than that in the wild-type ATCC13032 strain, which we determined using both next-generation RNA sequencing and quantitative real-time PCR analysis. When we disrupted the bioB gene in C. glutamicum ATCC21300, l-lysine production decreased by approximately 76%, and the three genes involved in biotin transport (NCgl1883, NCgl1884, and NCgl1885) were significantly downregulated. These results will be helpful to improve our understanding of C. glutamicum for industrial amino acid production.
Highlights
Corynebacterium glutamicum is widely used for the biotechnological production of industrially important amino acids, such as L-glutamate and L-lysine [1,2]
C. glutamicum ATCC21300, L-lysine production decreased by approximately 76%, and the three genes involved in biotin transport (NCgl1883, NCgl1884, and NCgl1885) were significantly downregulated
Since the first use of C. glutamicum to commercially produce L-lysine, various approaches to improve the production of L-lysine were investigated
Summary
Corynebacterium glutamicum is widely used for the biotechnological production of industrially important amino acids, such as L-glutamate and L-lysine [1,2]. After discovering that C. glutamicum can secrete amino acids, many researchers have attempted to develop an industrial strain by a classical random mutagenesis approach [3]. Mutants derived from random mutagenesis are generally inferior to their wild-type strains concerning industrially important properties, such as their growth, sugar consumption, and stress tolerance. These limitations have generally restricted the establishment of highly productive industrial strains [1]. Our findings provide insight into the general physiology of the cells, specific amino acid production mechanisms in C. glutamicum, and potential advances in the rational amino acid production mechanisms in C. glutamicum, engineering of industrially advantageous strains. Our findings provide insight into the general physiology of the cells, specific amino acid production mechanisms in C. glutamicum, and potential advances in the rational amino acid production mechanisms in C. glutamicum, engineering of industrially advantageous strains. and potential advances in the rational engineering of industrially advantageous strains
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