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J Bacteriol, April 1998, p. 1642-1646, Vol. 180, No. 7
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

An Archaeal Aerotaxis Transducer Combines Subunit I Core Structures of Eukaryotic Cytochrome c Oxidase and Eubacterial Methyl-Accepting Chemotaxis Proteins

Alexei Brooun,1 James Bell,2 Tracey Freitas,1 Randy W. Larsen,2 and Maqsudul Alam1,*

Department of Microbiology1 and Department of Chemistry,2 University of Hawaii, Honolulu, Hawaii 96822

Received 31 October 1997/Accepted 30 December 1997

Signal transduction in the archaeon Halobacterium salinarum is mediated by three distinct subfamilies of transducer proteins. Here we report the complete htrVIII gene sequence and present analysis of the encoded primary structure and its functional features. HtrVIII is a 642-amino-acid protein and belongs to halobacterial transducer subfamily B. At the N terminus, the protein contains six transmembrane segments that exhibit homology to the heme-binding sites of the eukaryotic cytochrome c oxidase. The C-terminal domain has high homology with the eubacterial methyl-accepting chemotaxis protein. The HtrVIII protein mediates aerotaxis: a strain with a deletion of the htrVIII gene loses aerotaxis, while an overproducing strain exhibits stronger aerotaxis. We also demonstrate that HtrVIII is a methyl-accepting protein and demethylates during the aerotaxis response.

* Corresponding author. Mailing address: Department of Microbiology, Snyder Hall 207, 2538 The Mall, University of Hawaii, Honolulu, HI 96822. Phone: (808) 956-8553. Fax: (808) 956-5339. E-mail: alam{at}hawaii.edu.




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