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| Home > Publications database > Physiology and global gene expression of a Corynebacterium glutamicum ΔF1FO-ATP synthase mutant devoid of oxidative phosphorylation > print |
| 001 | 20870 | ||
| 005 | 20180208194459.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:22050934 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.bbabio.2011.10.006 |
| 024 | 7 | _ | |2 WOS |a WOS:000300265300013 |
| 037 | _ | _ | |a PreJuSER-20870 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-Juel1)128970 |a Koch-Koerfges, A. |b 0 |u FZJ |
| 245 | _ | _ | |a Physiology and global gene expression of a Corynebacterium glutamicum ΔF1FO-ATP synthase mutant devoid of oxidative phosphorylation |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2012 |
| 300 | _ | _ | |a 370 - 380 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 802 |a Biochimica et Biophysica Acta |v 1817 |x 0006-3002 |y 2 |
| 500 | _ | _ | |a Financial support (grant 0315598 to MB and KM) by the Bundesministerium fur Bildung und Forschung (BMBF) is gratefully acknowledged. The authors would like to thank Dr. Melanie Brocker for the help with MALDI-TOF-MS measurements, Brita Weil and Ulrike Viets for excellent technical assistance, and Prof. Reinhard Kramer (Universitat zu Koln) for his support of the measurements of bioenergetic parameters. |
| 520 | _ | _ | |a A mutant of Corynebacterium glutamicum ATCC 13032 with a deletion of the atpBEFHAGDC genes encoding F(1)F(O)-ATP synthase was characterized. Whereas no growth was observed with acetate as sole carbon source, the ΔF(1)F(O) mutant reached 47% of the growth rate and 65% of the biomass of the wild type during shake-flask cultivation in glucose minimal medium. Initially, the mutant strain showed a strongly increased glucose uptake rate accompanied by a high oxygen consumption rate and pyruvate secretion into the medium. When oxygen became limiting, the glucose consumption rate was reduced below that of the wild type and pyruvate was consumed again. The ΔF(1)F(O) mutant had increased levels of b- and d-type cytochromes and a significantly increased proton motive force. Transcription of genes involved in central carbon metabolism was essentially unchanged, whereas genes for cytochrome bd oxidase, pyruvate:quinone oxidoreductase, oxidative stress response, and others showed increased mRNA levels. On the other hand, genes for amino acid biosynthesis and ribosomal proteins as well as many genes involved in transport displayed decreased mRNA levels. Several of the transcriptional changes were reflected at the protein level, but there were also discrepancies between the mRNA and protein levels suggesting some kind of posttranscriptional regulation. The results prove for the first time that F(1)F(O)-ATP synthase and oxidative phosphorylation are in general not essential for growth of C. glutamicum. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK410 |2 G:(DE-HGF) |a Biotechnologie |c PBT |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Acids: metabolism |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: genetics |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: growth & development |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: metabolism |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: physiology |
| 650 | _ | 2 | |2 MeSH |a Electron Transport: drug effects |
| 650 | _ | 2 | |2 MeSH |a Electron Transport: genetics |
| 650 | _ | 2 | |2 MeSH |a Electron Transport: physiology |
| 650 | _ | 2 | |2 MeSH |a Gene Expression Profiling |
| 650 | _ | 2 | |2 MeSH |a Gene Expression Regulation, Bacterial: drug effects |
| 650 | _ | 2 | |2 MeSH |a Glucose: metabolism |
| 650 | _ | 2 | |2 MeSH |a Glucose: pharmacology |
| 650 | _ | 2 | |2 MeSH |a Glycogen: metabolism |
| 650 | _ | 2 | |2 MeSH |a Organisms, Genetically Modified |
| 650 | _ | 2 | |2 MeSH |a Oxidative Phosphorylation |
| 650 | _ | 2 | |2 MeSH |a Oxygen Consumption: genetics |
| 650 | _ | 2 | |2 MeSH |a Oxygen Consumption: physiology |
| 650 | _ | 2 | |2 MeSH |a Proteome: analysis |
| 650 | _ | 2 | |2 MeSH |a Proteome: metabolism |
| 650 | _ | 2 | |2 MeSH |a Proton-Translocating ATPases: genetics |
| 650 | _ | 2 | |2 MeSH |a Proton-Translocating ATPases: physiology |
| 650 | _ | 2 | |2 MeSH |a Sequence Deletion |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Acids |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Proteome |
| 650 | _ | 7 | |0 50-99-7 |2 NLM Chemicals |a Glucose |
| 650 | _ | 7 | |0 9005-79-2 |2 NLM Chemicals |a Glycogen |
| 650 | _ | 7 | |0 EC 3.6.3.14 |2 NLM Chemicals |a Proton-Translocating ATPases |
| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a F1FO-ATP synthase |
| 653 | 2 | 0 | |2 Author |a Oxidative phosphorylation |
| 653 | 2 | 0 | |2 Author |a atpBEFHAGDC deletion |
| 653 | 2 | 0 | |2 Author |a Corynebacterium glutamicum |
| 653 | 2 | 0 | |2 Author |a Proton motive force |
| 653 | 2 | 0 | |2 Author |a Gene expression |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Kabus, A. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Ochrombel, I. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Marin, K. |b 3 |
| 700 | 1 | _ | |0 P:(DE-Juel1)128943 |a Bott, M. |b 4 |u FZJ |
| 773 | _ | _ | |0 PERI:(DE-600)1460387-1 |a 10.1016/j.bbabio.2011.10.006 |g Vol. 1817, p. 370 - 380 |p 370 - 380 |q 1817<370 - 380 |t Biochimica et biophysica acta |v 1817 |x 0006-3002 |y 2012 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1016/j.bbabio.2011.10.006 |
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| 914 | 1 | _ | |y 2012 |
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