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Roles of Three Histidine Kinase Genes in Hyphal Development and Virulence of the Pathogenic Fungus Candida albicans
Results imply that in C. albicans, CaSLN1 and CaNIK1 function upstream of CaHK1 but are in distinct signal transmission pathways.
Isolation of CaSLN1 and CaNIK1, the genes for osmosensing histidine kinase homologues, from the pathogenic fungus Candida albicans.
SLN1 of Candida albicans was functionally cloned using an S. cerevisiae strain in which SLN1 expression was conditionally suppressed andletion analysis of the cloned gene demonstrated that the receiver domain of C.Albicans Sln1p was not necessary to rescue SLN 1-deficient S. Cerevisiae strains.
Saccharomyces cerevisiae GNA1, an Essential Gene Encoding a Novel Acetyltransferase Involved in UDP-N-acetylglucosamine Synthesis*
- T. Mio, T. Yamada-Okabe, M. Arisawa, H. Yamada‐Okabe
- Biology, ChemistryThe Journal of Biological Chemistry
- 1 January 1999
Results indicate that YFL017C specifies glucosamine-6-phosphate acetyltransferase; therefore, the gene was designated GNA1(glucosamines- 6-ph phosphateacetyl transferase), whereas bacterial phosphoglucosamine acetyl transferring activities are intrinsic in a single polypeptide.
Cloning of the Candida albicans homolog of Saccharomyces cerevisiae GSC1/FKS1 and its involvement in beta-1,3-glucan synthesis
Results demonstrate that C. albicans GSC1 is the gene for a subunit of beta-1,3-glucan synthase.
Isolation of the Candida albicans homologs of Saccharomyces cerevisiae KRE6 and SKN1: expression and physiological function
- T. Mio, T. Yamada-Okabe, T. Yabe, T. Nakajima, M. Arisawa, H. Yamada‐Okabe
- BiologyJournal of bacteriology
- 1 April 1997
The results of Northern blot analysis revealed that C. albicans KRE6 was expressed at a higher level than SKN1 in the yeast phase, while SKn1 expression was strongly induced upon induction of hyphal formation, demonstrating that KRE 6 plays important roles in beta-1,6-glucan synthesis and budding in C.Albicans.
Isolation and Functional Analysis of a Gene, tcsB, Encoding a Transmembrane Hybrid-Type Histidine Kinase from Aspergillus nidulans
- Kentaro Furukawa, Y. Katsuno, T. Nakajima
- BiologyApplied and Environmental Microbiology
- 1 November 2002
The results suggest that A. nidulans has more complex and robust osmoregulatory systems than the yeast SLN1-HOG1 MAPK cascade, and imply that TcsB functions as an osmosensor histidine kinase.
Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans.
- T. Yamada-Okabe, O. Shimmi, R. Doi, K. Mizumoto, M. Arisawa, H. Yamada‐Okabe
- 1 September 1996
The mRNA-capping enzyme (mRNA 5'-guanylyltransferase) gene was cloned from a Candida albicans genomic DNA library by functional complementation of a Saccharomyces cerevisiae ceg1 delta null mutation, demonstrating that CGT1 is the C.Albicans mRNA 5-guanyl transferase gene.
Crystal Structure of Uridine-diphospho-N-acetylglucosamine Pyrophosphorylase from Candida albicans and Catalytic Reaction Mechanism*
A magnesium ion enhances the enzymatic activity of CaUAP1, and thus it is proposed that the magnesium ion increases the affinity between UTP and the enzyme by coordinating to the α- and γ-phosphate group of UTP.
Identification and characterization of the genes for N-acetylglucosamine kinase and N-acetylglucosamine-phosphate deacetylase in the pathogenic fungus Candida albicans.
- T. Yamada-Okabe, Y. Sakamori, T. Mio, H. Yamada‐Okabe
- BiologyEuropean journal of biochemistry
- 15 April 2001
Results clearly demonstrate that CaNAG2 and CaNAg5 encode GlcNAcP deacetylase and Glc NAc kinase, respectively, which appears to be closely associated with the virulence of C. albicans.
The yeast Chs4 protein stimulates the trypsin-sensitive activity of chitin synthase 3 through an apparent protein-protein interaction.
It was demonstrated that stimulation of non-zymogenic Chs3p activity by Chs 4p requires the amino acid region from 269 to 563 of Chs4p, and it seems that Chs5p activates Chs2p through protein-protein interaction and not the EF-hand motif nor a possible prenylation site in Chs6p.