Regulation of ldh expression during biotin-limited growth of Corynebacterium glutamicum
| Autor: | Christiane Dietrich, Pierre Maréchal, Armel Guyonvarch, Aimé Nato, Bruno Bost |
|---|---|
| Přispěvatelé: | Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Time Factors
Transcription Genetic Mutant Molecular Sequence Data Biotin Dehydrogenase Electrophoretic Mobility Shift Assay Biology Microbiology Corynebacterium glutamicum 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Lactic Acid Promoter Regions Genetic ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences Binding Sites Base Sequence L-Lactate Dehydrogenase 030306 microbiology Effector Fructose Metabolism PEP group translocation Gene Expression Regulation Bacterial Molecular biology Culture Media [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Biochemistry chemistry Mutagenesis Site-Directed |
| Zdroj: | Microbiology Microbiology, Microbiology Society, 2009, 155 (4), pp.1360-1375 Microbiology, Microbiology Society, 2009, 155 (4), pp.1360-75. ⟨10.1099/mic.0.022004-0⟩ |
| ISSN: | 1350-0872 1465-2080 |
| DOI: | 10.1099/mic.0.022004-0⟩ |
| Popis: | Corynebacterium glutamicumis a biotin-auxotrophic bacterium and some strains efficiently produce glutamic acid under biotin-limiting conditions. In an effort to understandC. glutamicummetabolism under biotin limitation, growth of the type strain ATCC 13032 was investigated in batch cultures and a time-course analysis was performed. A transient excretion of organic acids was observed and we focused our attention on lactate synthesis. Lactate synthesis was due to theldh-encodedl-lactate dehydrogenase (Ldh). Features of Ldh activity andldhtranscription were analysed. Theldhgene was shown to be regulated at the transcriptional level by SugR, a pleiotropic transcriptional repressor also acting on most phosphotransferase system (PTS) genes. Electrophoretic mobility shift assays (EMSAs) and site-directed mutagenesis allowed the identification of the SugR-binding site. Effector studies using EMSAs and analysis ofldhexpression in aptsFmutant revealed fructose 1-phosphate as a highly efficient negative effector of SugR. Fructose 1,6-bisphosphate also affected SugR binding. |
| Databáze: | OpenAIRE |
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