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Journal of Bacteriology, May 2002, p. 2491-2499, Vol. 184, No. 9
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.9.2491-2499.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Newly Identified Cytochrome c Oxidase Operon in the Nitrogen-Fixing Cyanobacterium Anabaena sp. Strain PCC 7120 Specifically Induced in Heterocysts

Kathryn M. Jones* and Robert Haselkorn

Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, Illinois 60637

Received 17 July 2001/ Accepted 21 January 2002

Two operons have been cloned from Anabaena sp. strain PCC 7120 DNA, each of which encodes the three core subunits of distinct mitochondrial-type cytochrome c oxidases. The two operons are only 72 to 85% similar to one another at the nucleotide level in the most conserved subunit. One of these, coxBACII, is induced >20-fold in the middle to late stages of heterocyst differentiation. Analysis of green fluorescent protein reporters indicates that this operon is expressed specifically in proheterocysts and heterocysts. The other operon, coxBACI, is induced only 2.5-fold following nitrogen step-down and is expressed in all cells. Surprisingly, a disruption mutant of coxAII, the gene encoding subunit I of the heterocyst-specific oxidase, grows normally in the absence of combined nitrogen. It is likely that coxBACI and/or two other putative terminal oxidases present in the Anabaena sp. strain PCC 7120 genome are able to compensate for the loss of the heterocyst-specific oxidase in providing ATP for nitrogen fixation and maintaining a low oxygen level in heterocysts.

* Corresponding author. Present address: Department of Molecular Genetics and Cell Biology, University of Chicago, 920 East 58th St., Chicago, IL 60637. Phone: (773) 702-1081. Fax: (773) 702-3172. E-mail: kmj5{at}midway.uchicago.edu.

Journal of Bacteriology, May 2002, p. 2491-2499, Vol. 184, No. 9
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.9.2491-2499.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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