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Eukaryotic Cell, December 2003, p. 1151-1161, Vol. 2, No. 6
1535-9778/03/$08.00+0 DOI: 10.1128/EC.2.6.1151-1161.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Olen C. Yoder,
and B. Gillian Turgeon*
Torrey Mesa Research Institute/Syngenta Research and Technology, San Diego, California 92121
Received 14 March 2003/ Accepted 16 July 2003
Two-component phosphorelay systems are minimally comprised of a histidine kinase (HK) component, which autophosphorylates in response to an environmental stimulus, and a response regulator (RR) component, which transmits the signal, resulting in an output such as activation of transcription, or of a mitogen-activated protein kinase cascade. The genomes of the yeasts Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Candida albicans encode one, three, and three HKs, respectively. In contrast, the genome sequences of the filamentous ascomycetes Neurospora crassa, Cochliobolus heterostrophus (Bipolaris maydis), Gibberella moniliformis (Fusarium verticillioides), and Botryotinia fuckeliana (Botrytis cinerea) encode an extensive family of two-component signaling proteins. The putative HKs fall into 11 classes. Most of these classes are represented in each filamentous ascomycete species examined. A few of these classes are significantly more prevalent in the fungal pathogens than in the saprobe N. crassa, suggesting that these groups contain paralogs required for virulence. Despite the larger numbers of HKs in filamentous ascomycetes than in yeasts, all of the ascomycetes contain virtually the same downstream histidine phosphotransfer proteins and RR proteins, suggesting extensive cross talk or redundancy among HKs.
Present address: Plant and Microbial Biology Department, University of California, Berkeley, CA 94720.
Present address: Diversa Corporation, San Diego, CA 92121.
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