AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Stansen, C.
Right arrow Articles by Wendisch, V. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stansen, C.
Right arrow Articles by Wendisch, V. F.
Agricola
Right arrow Articles by Stansen, C.
Right arrow Articles by Wendisch, V. F.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, October 2005, p. 5920-5928, Vol. 71, No. 10
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.10.5920-5928.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of a Corynebacterium glutamicum Lactate Utilization Operon Induced during Temperature-Triggered Glutamate Production{dagger}

Corinna Stansen,1 Davin Uy,2 Stephane Delaunay,2 Lothar Eggeling,1 Jean-Louis Goergen,2 and Volker F. Wendisch1*

Institute of Biotechnology 1, Research Center Juelich, D-52428 Juelich, Germany,1 Laboratoire des Sciences du Genie Chimique, Institut National Polytechnique de Lorraine, 54505 Vandoeuvre-les-Nancy, France2

Received 18 March 2005/ Accepted 6 May 2005

Gene expression changes of glutamate-producing Corynebacterium glutamicum were identified in transcriptome comparisons by DNA microarray analysis. During glutamate production induced by a temperature shift, C. glutamicum strain 2262 showed significantly higher mRNA levels of the NCgl2816 and NCgl2817 genes than its non-glutamate-producing derivative 2262NP. Reverse transcription-PCR analysis showed that the two genes together constitute an operon. NCgl2816 putatively codes for a lactate permease, while NCgl2817 was demonstrated to encode quinone-dependent L-lactate dehydrogenase, which was named LldD. C. glutamicum LldD displayed Michaelis-Menten kinetics for the substrate L-lactate with a Km of about 0.51 mM. The specific activity of LldD was about 10-fold higher during growth on L-lactate or on an L-lactate-glucose mixture than during growth on glucose, D-lactate, or pyruvate, while the specific activity of quinone-dependent D-lactate dehydrogenase differed little with the carbon source. RNA levels of NCgl2816 and lldD were about 18-fold higher during growth on L-lactate than on pyruvate. Disruption of the NCgl2816-lldD operon resulted in loss of the ability to utilize L-lactate as the sole carbon source. Expression of lldD restored L-lactate utilization, indicating that the function of the permease gene NCgl2816 is dispensable, while LldD is essential, for growth of C. glutamicum on L-lactate.


* Corresponding author. Mailing address: Institute of Biotechnology 1, Research Centre Juelich, D-52425 Juelich, Germany. Phone: 49-2461-615169. Fax: 49-2461-612710. E-mail: v.wendisch{at}fz-juelich.de.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.


Applied and Environmental Microbiology, October 2005, p. 5920-5928, Vol. 71, No. 10
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.10.5920-5928.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 2005 by the American Society for Microbiology. All rights reserved.