AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Brouwers, G.-J.
Right arrow Articles by de Vrind-de Jong, E. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Brouwers, G.-J.
Right arrow Articles by de Vrind-de Jong, E. W.
Agricola
Right arrow Articles by Brouwers, G.-J.
Right arrow Articles by de Vrind-de Jong, E. W.

Applied and Environmental Microbiology, April 1999, p. 1762-1768, Vol. 65, No. 4
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

cumA, a Gene Encoding a Multicopper Oxidase, Is Involved in Mn2+ Oxidation in Pseudomonas putida GB-1

Geert-Jan Brouwers,1,* Johannes P. M. de Vrind,1 Paul L. A. M. Corstjens,1 Pierre Cornelis,2 Christine Baysse,2 and Elisabeth W. de Vrind-de Jong1

Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, 2300 R.A. Leiden, The Netherlands1 and Flanders Interuniversity Institute of Biotechnology, Department of Immunology, Paracytology and Ultrastructure, Vrije Universiteit Brussel, B-1640 Sint Genesius Rode, Belgium2

Received 21 August 1998/Accepted 15 January 1999

Pseudomonas putida GB-1-002 catalyzes the oxidation of Mn2+. Nucleotide sequence analysis of the transposon insertion site of a nonoxidizing mutant revealed a gene (designated cumA) encoding a protein homologous to multicopper oxidases. Addition of Cu2+ increased the Mn2+-oxidizing activity of the P. putida wild type by a factor of approximately 5. The growth rates of the wild type and the mutant were not affected by added Cu2+. A second open reading frame (designated cumB) is located downstream from cumA. Both cumA and cumB probably are part of a single operon. The translation product of cumB was homologous (level of identity, 45%) to that of orf74 of Bradyrhizobium japonicum. A mutation in orf74 resulted in an extended lag phase and lower cell densities. Similar growth-related observations were made for the cumA mutant, suggesting that the cumA mutation may have a polar effect on cumB. This was confirmed by site-specific gene replacement in cumB. The cumB mutation did not affect the Mn2+-oxidizing ability of the organism but resulted in decreased growth. In summary, our data indicate that the multicopper oxidase CumA is involved in the oxidation of Mn2+ and that CumB is required for optimal growth of P. putida GB-1-002.

* Corresponding author. Mailing address: Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, P.O. Box 9502, 2300 R.A. Leiden, The Netherlands. Phone: 31 71 5274707. Fax: 31 71 5274537. E-mail: brouwers{at}chem.leidenuniv.nl.

Applied and Environmental Microbiology, April 1999, p. 1762-1768, Vol. 65, No. 4
0099-2240/99/$04.00+0
Copyright © 1999, 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 © 1999 by the American Society for Microbiology. All rights reserved.