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Use of an Alternative Pathway for Isoleucine Synthesis in Threonine-Producing Strains of Escherichia coli

Authors
  • Vybornaya, T. V.1
  • Yuzbashev, T. V.1
  • Fedorov, A. S.1
  • Bubnov, D. M.1
  • Filippova, S. S.1
  • Bondarenko, F. V.1
  • Sineoky, S. P.1
  • 1 State Research Institute for Genetics and Selection of Industrial Microorganisms, Kurchatov Institute National Research Center (Kurchatov Institute NRC, GOSNIIGENETIKA), Moscow, 117545, Russia , Moscow (Russia)
Type
Published Article
Journal
Applied Biochemistry and Microbiology
Publisher
Pleiades Publishing
Publication Date
Dec 01, 2020
Volume
56
Issue
7
Pages
759–769
Identifiers
DOI: 10.1134/S0003683820070066
Source
Springer Nature
Keywords
License
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Abstract

AbstractAn E. coli strain in which all known pathways of threonine catabolism were inactivated (Δtdh, ΔltaE, ΔilvA, ΔtdcB, ΔyiaY) has been constructed. It was shown that the expression of heterologous citramalate synthase from Leptospira interrogans in an E. coli strain carrying the ΔilvA deletion can serve as an alternative pathway for isoleucine synthesis. It was observed that cimA overexpression has a negative effect on threonine production. We developed a system for regulated gene expression based on the inducible promoter PLtetO and TetR, a repressor of the tetracycline operon. The threonine-producing strain B-1201, in which the cimA gene is expressed under the control of the regulated promoter, was constructed. When the B-1201 strain was cultivated in a fermenter, a correlation was established between the threonine productivity and the expression level of the cimA gene, and the optimal inductor content for the maximum threonine accumulation was also determined.

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