Mutations in the fusA Gene Encoding Elongation Factor G in the Coryneform Bacterium Lead to Increased Lysine Production

• Published in: Applied biochemistry and microbiology Vol. 53; no. 8; pp. 781 - 785
• Main Authors: Tokmakova, I. P., Ryabchenko, L. E., Gerasimova, T. V., Kameneva, S. V., Yanenko, A. S.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01-12-2017; Springer Nature B.V
• Subjects: Acid resistance; Amino acids; Bacteria; Biochemistry; Biology; Biomedical and Life Sciences; Cloning; Corynebacterium glutamicum; Elongation; Fusidic acid; Gene Engineering; Gene sequencing; Glutamine; Histidine; Homologous recombination; Homology; Life Sciences; Lysine; Medical Microbiology; Microbiology; Mutation; Producers; Selection; mutations in; elongation factor G; L-lysine synthesis; gene; resistance to fusidic acid
• ISSN: 0003-6838; 1608-3024
• DOI: 10.1134/S0003683817080075

Resistance to fusidic acid in
Corynebacterium glutamicum
and
Brevibacterium flavum
is associated with mutations in the
fusA
gene, which encodes the elongation factor G (EF-G). Two to ten percent of fusidic acid-resistant clones were shown to produce more lysine than parent strains. Sequencing of the
fusA
gene in clones with a high level of lysine production made it possible to find two mutations in the gene at position 1383—С1383G and С1383А. These mutations cause amino acid replacement at position 461 in the protein EF-G, namely, histidine is substituted by glutamine (H461Q). The mutation С1383G was introduced in the chromosomal copy of the
fusA
gene in
C. glutamicum
and
B. flavum
strains by homologous recombination. All clones containing the mutant variant of the
fusA
gene produced 10% more lysine than the parent strains.