Isolation of CaSLN1 and CaNIK1, the genes for osmosensing histidine kinase homologues, from the pathogenic fungus Candida albicans.
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.
Nagahashi
Shigehisa
S
Department of Mycology, Nippon Roche Research Center, 200 Kajiwara, Kamakura, Kanagawa 247, Japan.|Department of Biology, McGill University, 1205 Dr. Penfield, Montreal, Quebec, Canada H3A 1B1.
Mio
Toshiyuki
T
Department of Mycology, Nippon Roche Research Center, 200 Kajiwara, Kamakura, Kanagawa 247, Japan.
Ono
Naomi
N
Department of Mycology, Nippon Roche Research Center, 200 Kajiwara, Kamakura, Kanagawa 247, Japan.
Yamada-Okabe
Toshiko
T
Department of Hygiene, School of Medicine, Yokohama City University, 3-9, Fukuura, Kanazawaku, Yokohama 236, Japan.
Arisawa
Mikio
M
Department of Mycology, Nippon Roche Research Center, 200 Kajiwara, Kamakura, Kanagawa 247, Japan.
Bussey
Howard
H
Department of Biology, McGill University, 1205 Dr. Penfield, Montreal, Quebec, Canada H3A 1B1.
Yamada-Okabe
Hisafumi
H
Department of Mycology, Nippon Roche Research Center, 200 Kajiwara, Kamakura, Kanagawa 247, Japan.
D000595:Amino Acid Sequence; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000235:genetics / Q000378:metabolism; D002176:Candida albicans / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004271:DNA, Fungal / Q000032:analysis / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism; D005800:Genes, Fungal; D005816:Genetic Complementation Test; D000071677:Histidine Kinase; D047908:Intracellular Signaling Peptides and Proteins; D020928:Mitogen-Activated Protein Kinases; D008969:Molecular Sequence Data; D009995:Osmosis; D010957:Plasmids; D011494:Protein Kinases / Q000235:genetics* / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D004271:DNA, Fungal; D005656:Fungal Proteins; D047908:Intracellular Signaling Peptides and Proteins; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases; C106494:HSL1 protein, S cerevisiae; D017346:Protein Serine-Threonine Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; C088589:HOG1 protein, S cerevisiae; D020928:Mitogen-Activated Protein Kinases; D000071677:Histidine Kinase; C083749:SLN1 protein, S cerevisiae