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 Alexandre, G.
Right arrow Articles by Zhulin, I. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Alexandre, G.
Right arrow Articles by Zhulin, I. B.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 1999, p. 6730-6738, Vol. 181, No. 21
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Loss of Cytochrome c Oxidase Activity and Acquisition of Resistance to Quinone Analogs in a Laccase-Positive Variant of Azospirillum lipoferum

Gladys Alexandre,1,2 René Bally,1 Barry L. Taylor,2 and Igor B. Zhulin2,*

Laboratoire d'Ecologie Microbienne du Sol, CNRS-UMR 5557, l'Universite Claude-Bernard, 69622 Villeurbanne Cedex, France,1 and Department of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, California 923502

Received 26 April 1999/Accepted 23 August 1999

Laccase, a p-diphenol oxidase typical of plants and fungi, has been found recently in a proteobacterium, Azospirillum lipoferum. Laccase activity was detected in both a natural isolate and an in vitro-obtained phase variant that originated from the laccase-negative wild type. In this study, the electron transport systems of the laccase-positive variant and its parental laccase-negative forms were compared. During exponential (but not stationary) growth under fully aerobic (but not under microaerobic) conditions, the laccase-positive variant lost a respiratory branch that is terminated in a cytochrome c oxidase of the aa3 type; this was most likely due to a defect in the biosynthesis of a heme component essential for the oxidase. The laccase-positive variant was significantly less sensitive to the inhibitory action of quinone analogs and fully resistant to inhibitors of the bc1 complex, apparently due to the rearrangements of its respiratory system. We propose that the loss of the cytochrome c oxidase-containing branch in the variant is an adaptive strategy to the presence of intracellular oxidized quinones, the products of laccase activity.


* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA 92350. Phone: (909) 558-4480. Fax: (909) 558-4035. E-mail: izhulin{at}som.llu.edu.


Journal of Bacteriology, November 1999, p. 6730-6738, Vol. 181, No. 21
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Wasim, M., Bible, A. N., Xie, Z., Alexandre, G. (2009). Alkyl hydroperoxide reductase has a role in oxidative stress resistance and in modulating changes in cell-surface properties in Azospirillum brasilense Sp245. Microbiology 155: 1192-1202 [Abstract] [Full Text]  
  • Alexandre, G., Zhulin, I. B. (2001). More Than One Way To Sense Chemicals. J. Bacteriol. 183: 4681-4686 [Full Text]  
  • Alexandre, G., Greer, S. E., Zhulin, I. B. (2000). Energy Taxis Is the Dominant Behavior in Azospirillum brasilense. J. Bacteriol. 182: 6042-6048 [Abstract] [Full Text]  
  • Solano, F., Lucas-Elío, P., Fernández, E., Sanchez-Amat, A. (2000). Marinomonas mediterranea MMB-1 Transposon Mutagenesis: Isolation of a Multipotent Polyphenol Oxidase Mutant. J. Bacteriol. 182: 3754-3760 [Abstract] [Full Text]