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Single-gene knockout of a novel regulatory element confers ethionine resistance and elevates methionine production in Corynebacterium glutamicum

Mampel, Jörg ; Schröder, Hartwig ; Haefner, Stefan ; Sauer, Uwe

In: Applied Microbiology and Biotechnology, 2005, vol. 68, no. 2, p. 228-236

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    Titre
    • Single-gene knockout of a novel regulatory element confers ethionine resistance and elevates methionine production in Corynebacterium glutamicum
    Auteur
    • Mampel, Jörg. Institute of Biotechnology, Swiss Federal Institute of Technology (ETH), 8093, Zurich, Switzerland
    • Schröder, Hartwig. BASF Aktiengesellschaft, 67056, Ludwigshafen, Germany
    • Haefner, Stefan. BASF Aktiengesellschaft, 67056, Ludwigshafen, Germany
    • Sauer, Uwe. Institute of Biotechnology, Swiss Federal Institute of Technology (ETH), 8093, Zurich, Switzerland
    Type de document
    • Postprint
    Langue
    • Inglese
    Publié dans
    • Applied Microbiology and Biotechnology, 2005, vol. 68, no. 2, p. 228-236. Springer-Verlag; http://www.springer.de
    Autre version électronique
    Classification
    • Biotechnologies
    Identifiant OAI-PMH
    • oai:doc.rero.ch:321514
    Summary
    Despite the availability of genome data and recent advances in methionine regulation in Corynebacterium glutamicum, sulfur metabolism and its underlying molecular mechanisms are still poorly characterized in this organism. Here, we describe the identification of an ORF coding for a putative regulatory protein that controls the expression of genes involved in sulfur reduction dependent on extracellular methionine levels. C. glutamicum was randomly mutagenized by transposon mutagenesis and 7,000 mutants were screened for rapid growth on agar plates containing the methionine antimetabolite d,l-ethionine. In all obtained mutants, the site of insertion was located in the ORF NCgl2640 of unknown function that has several homologues in other bacteria. All mutants exhibited similar ethionine resistance and this phenotype could be transferred to another strain by the defined deletion of the NCgl2640 gene. Moreover, inactivation of NCgl2640 resulted in significantly increased methionine production. Using promoter lacZ-fusions of genes involved in sulfur metabolism, we demonstrated the relief of l-methionine repression in the NCgl2640 mutant for cysteine synthase, o-acetylhomoserine sulfhydrolase (metY) and sulfite reductase. Complementation of the mutant strain with plasmid-borne NCgl2640 restored the wild-type phenotype for metY and sulfite reductase