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microbiology, Vol 144, 425-432, Copyright © 1998 by Society for General Microbiology
ARTICLES |
S Nagahashi, T Mio, N Ono, T Yamada-Okabe, M Arisawa, H Bussey and H Yamada-Okabe
Department of Biology, McGill University, Montreal, Quebec, Canada.
Recent studies have revealed that fungi possess a mechanism similar to bacterial two-component systems to respond to extracellular changes in osmolarity. In Saccharomyces cerevisiae, Sln1p contains both histidine kinase and receiver (response regulator) domains and acts as an osmosensor protein that regulates the downstream HOG1 MAP kinase cascade. SLN1 of Candida albicans was functionally cloned using an S. cerevisiae strain in which SLN1 expression was conditionally suppressed. Deletion analysis of the cloned gene demonstrated that the receiver domain of C. albicans Sln1p was not necessary to rescue SLN1- deficient S. cerevisiae strains. Unlike S. cerevisiae, a null mutation of C. albicans SLN1 was viable under regular and high osmotic conditions, but it caused a slight growth retardation at high osmolarity. Southern blotting with C. albicans SLN1 revealed the presence of related genes, one of which is highly homologous to the NIK1 gene of Neurospora crassa. Thus, C. albicans harbours both SLN1- and NIK1-type histidine kinases.
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