Control of adhA and sucR expression by the SucR regulator in Corynebacterium glutamicum

• Published in: Journal of biotechnology Vol. 152; no. 3; pp. 77 - 86
• Main Authors: Auchter, Marc, Laslo, Tanja, Fleischer, Constanze, Schiller, Laura, Arndt, Annette, Gaigalat, Lars, Kalinowski, Jörn, Eikmanns, Bernhard J.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 20.03.2011; Elsevier
• Subjects: Alcohol dehydrogenase; Alcohol Dehydrogenase - genetics; Alcohol Dehydrogenase - metabolism; autoregulation; Bacterial Proteins - genetics; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Base Sequence; Binding; Binding Sites; Biological and medical sciences; Biotechnology; Carbon; Control; Corynebacterium glutamicum; Corynebacterium glutamicum - enzymology; Corynebacterium glutamicum - genetics; DNA, Bacterial - genetics; Ethanol metabolism; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Bacterial; Gene Silencing; Genes; Genes, Bacterial - genetics; Genetic Loci - genetics; Molecular Sequence Data; operon; Plasmids - genetics; promoter regions; Promoter Regions, Genetic - genetics; Protein Binding; Regulators; repressor proteins; sequence analysis; SucR transcriptional regulator; Transcription, Genetic; Transcriptional regulation; SucR transcriptional regulator; Alcohol dehydrogenase; Transcriptional regulation; Corynebacterium glutamicum; Ethanol metabolism; Ethanol; Transcription; Enzyme; Regulator; Metabolism; Regulation(control); Bacteria; Actinomycetes; Corynebacteriaceae; Oxidoreductases; Transcription factor
• ISSN: 0168-1656; 1873-4863
• DOI: 10.1016/j.jbiotec.2011.02.003

The alcohol dehydrogenase gene adhA in Corynebacterium glutamicum is subject to a complex carbon source-dependent regulation mediated by RamA, RamB and GlxR. In this study we identified SucR as the fourth transcriptional regulator involved in expression control of the adhA gene. SucR specifically binds to the adhA promoter and acts as transcriptional repressor independent of the carbon source used. Furthermore, we found that SucR negatively controls the expression of its own gene. This negative autoregulation is mediated by binding of SucR to at least one of four identified binding sites located in the promoter region of sucR. EMSA experiments and subsequent sequence analysis led to the identification of the SucR consensus binding sequence YYAACAWMAW. This binding motif is different from the binding site (ACTCTAGGGG) recently described for SucR in the promoter region of the sucCD operon. However, we were not able to detect a specific interaction of purified SucR protein with this motif present in the sucCD promoter region.