This title appears in the Scientific Report :
2005
Please use the identifier:
http://hdl.handle.net/2128/2422 in citations.
Please use the identifier: http://dx.doi.org/10.1128/AEM.71.10.5920-5928.2005 in citations.
Characterization of a Corynebacterium glutamicum lactate utilization operon induced during temperature-triggered glutamate production
Characterization of a Corynebacterium glutamicum lactate utilization operon induced during temperature-triggered glutamate production
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 NCgl281...
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Personal Name(s): | Stansen, K. |
---|---|
Uy, D. / Delaunay, S. / Eggeling, L. / Goergen, J. L. / Wendisch, V. F. | |
Contributing Institute: |
Biotechnologie 1; IBT-1 |
Published in: | Applied and environmental microbiology, 71 (2005) S. 5920 - 5928 |
Imprint: |
Washington, DC [u.a.]
Soc.
2005
|
Physical Description: |
5920 - 5928 |
DOI: |
10.1128/AEM.71.10.5920-5928.2005 |
PubMed ID: |
16204505 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Applied and Environmental Microbiology
71 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1128/AEM.71.10.5920-5928.2005 in citations.
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 K(m) 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. |