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Journal of Bacteriology, February 2006, p. 1341-1350, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1341-1350.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Pyruvate:Quinone Oxidoreductase in Corynebacterium glutamicum: Molecular Analysis of the pqo Gene, Significance of the Enzyme, and Phylogenetic Aspects

Mark E. Schreiner, Christian Riedel,{ddagger} Jiri Holátko,{dagger} Miroslav Pátek,{dagger} and Bernhard J. Eikmanns*

Department of Microbiology and Biotechnology, University of Ulm, 89069 Ulm, Germany

Received 12 August 2005/ Accepted 17 October 2005

Corynebacterium glutamicum recently has been shown to possess pyruvate:quinone oxidoreductase (PQO), catalyzing the oxidative decarboxylation of pyruvate to acetate and CO2 with a quinone as the electron acceptor. Here, we analyze the expression of the C. glutamicum pqo gene, investigate the relevance of the PQO enzyme for growth and amino acid production, and perform phylogenetic studies. Expression analyses revealed that transcription of pqo is initiated 45 bp upstream of the translational start site and that it is organized in an operon together with genes encoding a putative metal-activated pyridoxal enzyme and a putative activator protein. Inactivation of the chromosomal pqo gene led to the absence of PQO activity; however, growth and amino acid production were not affected under either condition tested. Introduction of plasmid-bound pqo into a pyruvate dehydrogenase complex-negative C. glutamicum strain partially relieved the growth phenotype of this mutant, indicating that high PQO activity can compensate for the function of the pyruvate dehydrogenase complex. To investigate the distribution of PQO enzymes in prokaryotes and to clarify the relationship between PQO, pyruvate oxidase (POX), and acetohydroxy acid synthase enzymes, we compiled and analyzed the phylogeny of respective proteins deposited in public databases. The analyses revealed a wide distribution of PQOs among prokaryotes, corroborated the hypothesis of a common ancestry of the three enzymes, and led us to propose that the POX enzymes of Lactobacillales were derived from a PQO.

* Corresponding author. Mailing address: Department of Microbiology and Biotechnology, University of Ulm, 89069 Ulm, Germany. Phone: 49 (0)731 50 22707. Fax: 49 (0) 731 50 22719. E-mail: bernhard.eikmanns{at}biologie.uni-ulm.de.

{ddagger} Present address: Dept. of Microbiology, Alimentary Pharmabiotic Centre, University College Cork, Cork, Ireland.

{dagger} Present address: Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídenská 1083, CZ-14220 Praha 4, Czech Republic.

Journal of Bacteriology, February 2006, p. 1341-1350, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1341-1350.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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