This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Georgi, T.
Right arrow Articles by Wendisch, V. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Georgi, T.
Right arrow Articles by Wendisch, V. F.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*1,4-BENZOQUINONE
*LACTIC ACID

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2008, p. 963-971, Vol. 190, No. 3
0021-9193/08/$08.00+0     doi:10.1128/JB.01147-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Regulation of L-Lactate Utilization by the FadR-Type Regulator LldR of Corynebacterium glutamicum{triangledown}

Tobias Georgi,1 Verena Engels,1 and Volker F. Wendisch2*

Institute of Biotechnology I, Research Center of Juelich, Juelich, Germany,1 Institute of Molecular Microbiology and Biotechnology, Westfalian Wilhelms University of Muenster, Muenster, Germany2

Received 20 July 2007/ Accepted 5 November 2007

Corynebacterium glutamicum can grow on L-lactate as a sole carbon and energy source. The NCgl2816-lldD operon encoding a putative transporter (NCgl2816) and a quinone-dependent L-lactate dehydrogenase (LldD) is required for L-lactate utilization. DNA affinity chromatography revealed that the FadR-type regulator LldR (encoded by NCgl2814) binds to the upstream region of NCgl2816-lldD. Overexpression of lldR resulted in strongly reduced NCgl2816-lldD mRNA levels and strongly reduced LldD activity, and as a consequence, a severe growth defect was observed in cells grown on L-lactate as the sole carbon and energy source, but not in cells grown on glucose, ribose, or acetate. Deletion of lldR had no effect on growth on these carbon sources but resulted in high NCgl2816-lldD mRNA levels and high LldD activity in the presence and absence of L-lactate. Purified His-tagged LldR bound to a 54-bp fragment of the NCgl2816-lldD promoter, which overlaps with the transcriptional start site determined by random amplification of cDNA ends-PCR and contains a putative operator motif typical of FadR-type regulators, which is –1TNGTNNNACNA10. Mutational analysis revealed that this motif with hyphenated dyad symmetry is essential for binding of LldD to the NCgl2816-lldD promoter. L-Lactate, but not D-lactate, interfered with binding of LldRHis to the NCgl2816-lldD promoter. Thus, during growth on media lacking L-lactate, LldR represses expression of NCgl2816-lldD. In the presence of L-lactate in the growth medium or under conditions leading to intracellular L-lactate accumulation, the L-lactate utilization operon is induced.

* Corresponding author. Mailing address: Institute of Molecular Microbiology and Biotechnology, Westfalian Wilhelms University of Muenster, Corrensstr. 3, D-48149 Muenster, Germany. Phone: 49-251-833 9827. Fax: 49-251-833 8388. E-mail: wendisch{at}uni-muenster.de

{triangledown} Published ahead of print on 26 November 2007.

Journal of Bacteriology, February 2008, p. 963-971, Vol. 190, No. 3
0021-9193/08/$08.00+0     doi:10.1128/JB.01147-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Youn, J.-W., Jolkver, E., Kramer, R., Marin, K., Wendisch, V. F. (2009). Characterization of the Dicarboxylate Transporter DctA in Corynebacterium glutamicum. J. Bacteriol. 191: 5480-5488 [Abstract] [Full Text]  
  • Toyoda, K., Teramoto, H., Inui, M., Yukawa, H. (2009). The ldhA Gene, Encoding Fermentative L-Lactate Dehydrogenase of Corynebacterium glutamicum, Is under the Control of Positive Feedback Regulation Mediated by LldR. J. Bacteriol. 191: 4251-4258 [Abstract] [Full Text]  
  • Kawaguchi, H., Sasaki, M., Vertes, A. A., Inui, M., Yukawa, H. (2009). Identification and Functional Analysis of the Gene Cluster for L-Arabinose Utilization in Corynebacterium glutamicum. Appl. Environ. Microbiol. 75: 3419-3429 [Abstract] [Full Text]  
  • Dietrich, C., Nato, A., Bost, B., Le Marechal, P., Guyonvarch, A. (2009). Regulation of ldh expression during biotin-limited growth of Corynebacterium glutamicum. Microbiology 155: 1360-1375 [Abstract] [Full Text]  
  • Engels, V., Lindner, S. N., Wendisch, V. F. (2008). The Global Repressor SugR Controls Expression of Genes of Glycolysis and of the L-Lactate Dehydrogenase LdhA in Corynebacterium glutamicum. J. Bacteriol. 190: 8033-8044 [Abstract] [Full Text]  
  • Gao, Y.-G., Suzuki, H., Itou, H., Zhou, Y., Tanaka, Y., Wachi, M., Watanabe, N., Tanaka, I., Yao, M. (2008). Structural and functional characterization of the LldR from Corynebacterium glutamicum: a transcriptional repressor involved in L-lactate and sugar utilization. Nucleic Acids Res 36: 7110-7123 [Abstract] [Full Text]  
  • Blancato, V. S., Repizo, G. D., Suarez, C. A., Magni, C. (2008). Transcriptional Regulation of the Citrate Gene Cluster of Enterococcus faecalis Involves the GntR Family Transcriptional Activator CitO. J. Bacteriol. 190: 7419-7430 [Abstract] [Full Text]  
  • Youn, J.-W., Jolkver, E., Kramer, R., Marin, K., Wendisch, V. F. (2008). Identification and Characterization of the Dicarboxylate Uptake System DccT in Corynebacterium glutamicum. J. Bacteriol. 190: 6458-6466 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»