{Reference Type}: Journal Article
{Title}: Molecular cloning, characterization and differential expression of DRK1             in Sporothrix schenckii.
{Author}: Hou B;Zhang Z;Zheng F;Liu X;
{Journal}: Int J Mol Med
{Volume}: 31
{Issue}: 1
{Year}: Jan 2013
{Factor}: 5.314
{DOI}: 10.3892/ijmm.2012.1193
{Abstract}: The dimorphism of Sporothrix schenckii (S. schenckii) reflects a developmental             switch in morphology and lifestyle that is necessary for virulence. DRK1, a hybrid             histidine kinase, functions as a global regulator of dimorphism and virulence             in Blastomyces dermatitidis (B. dermatitidis) and Histoplasma capsulatum (H. capsulatum).             The partial cDNA sequence of DRK1 of S. schenckii, designated SsDRK1, was obtained             using degenerate primers based on the conserved domain of the DRK1 of other fungi.             The complete cDNA sequence of SsDRK1 was obtained by 5' and 3' RACE. The full-length             cDNA is 4743 bp in size and has an open reading frame (ORF) of 4071 bp, encoding             1356 amino acid residues. The predicted molecular mass of SsDRK1 is 147.3 kDa             with an estimated theoretical isoelectric point of 5.46. The deduced amino acid             sequence of SsDRK1 shows 65% identity to that of B. dermatitidis. The SsDRK1 was             predicted to be a soluble histidine kinase and to contain three parts: sensor             domain, linker domain and functional domain. Quantitative real-time RT-PCR revealed             that SsDRK1 was more highly expressed in the yeast stage compared with that in             the mycelial stage, which indicated that the SsDRK1 may be involved in the dimorphic             switch in S. schenckii.