Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 147 (2001), 2437-2446
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
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, G. R.
Right arrow Articles by Clark, D. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, G. R.
Right arrow Articles by Clark, D. P.
Agricola
Right arrow Articles by Jiang, G. R.
Right arrow Articles by Clark, D. P.
Microbiology (2001), 147, 2437-2446.
© 2001 Society for General Microbiology


Physiology and Growth

Regulation of the ldhA gene, encoding the fermentative lactate dehydrogenase of Escherichia coli

Gene Ruijun Jianga,1, Sonia Nikolova1 and David P. Clark1

Department of Microbiology, Southern Illinois University, Carbondale, IL 62901-6508, USA1

Author for correspondence: David P. Clark. Tel: +1 618 453 3737. Fax: +1 618 453 8036. e-mail: clark{at}micro.siu.edu

The fermentative lactate dehydrogenase (LDH) of Escherichia coli is induced by low pH under anaerobic conditions. Both translational and transcriptional gene fusions to ldhA, which encodes the fermentative LDH, have now been made. Both types of ldhA–lacZ fusion were induced by low pH, but only in the absence of air. However, the translational fusions were consistently expressed at a five- to tenfold higher level than the transcriptional fusions, perhaps implying some post-transcriptional effect on ldhA expression. Introduction of arcB::Kan decreased expression of both translational and transcriptional ldhA–lacZ fusions by three- to fivefold. Disruption of mlc, which encodes a repressor of several genes of the phosphotransferase system, almost abolished expression of ldhA. Disruption of csrA caused a moderate drop in expression of both operon and protein ldhA fusions, whereas insertional inactivation of csrB or glgA had the opposite effect. These effects are probably indirect, resulting from alterations in sugar accumulation versus storage. Mutations in ptsG, cra, fnr, narL, rpoS, osmZ, appY, ack/pta, aceEF, pfl and ldhA had no effect on expression of the ldhA fusions. ldhA was not induced by the membrane-permeant weak acid benzoate, implying that it does not respond to the internal pH directly. Little pH induction was seen during growth on glycerol plus fumarate, suggesting that products of sugar fermentation are necessary for acid induction. Addition of succinate, acetate or lactate had no effect on ldhA expression. In contrast, pyruvate caused a two- to fourfold increase in expression of ldhA–lacZ. This accords with the idea that increased sugar metabolism indirectly induces ldhA.

Keywords: lactic acid, fermentation, anaerobic growth, CsrAB system, Mlc regulator, ArcAB system

Abbreviations: LDH, lactate dehydrogenase; PTS, phosphoenolpyruvate-dependent sugar phosphotransferase system

a Present address: Valentis, Inc., 863A Mitten Road, Burlingame, CA 94010, USA.




This article has been cited by other articles:


Home page
Microbiol. Mol. Biol. Rev.Home page
M.-J. Han and S. Y. Lee
The Escherichia coli Proteome: Past, Present, and Future Prospects
Microbiol. Mol. Biol. Rev., June 1, 2006; 70(2): 362 - 439.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
W. Chang, D. A. Small, F. Toghrol, and W. E. Bentley
Global Transcriptome Analysis of Staphylococcus aureus Response to Hydrogen Peroxide
J. Bacteriol., February 15, 2006; 188(4): 1648 - 1659.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
S. Zhou, K. T. Shanmugam, and L. O. Ingram
Functional Replacement of the Escherichia coliD-(-)-Lactate Dehydrogenase Gene (ldhA) with the L-(+)-Lactate Dehydrogenase Gene (ldhL) from Pediococcus acidilactici
Appl. Envir. Microbiol., April 1, 2003; 69(4): 2237 - 2244.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
T. Polen, D. Rittmann, V. F. Wendisch, and H. Sahm
DNA Microarray Analyses of the Long-Term Adaptive Response of Escherichia coli to Acetate and Propionate
Appl. Envir. Microbiol., March 1, 2003; 69(3): 1759 - 1774.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2001 Society for General Microbiology.