Identification of a putative transcription factor in Candida albicans that can complement the mating defect of Saccharomyces cerevisiae ste12 mutants.

作者：K. Malathi, Kaliannan Ganesan, Asis Datta · 发表于：Journal of Biological Chemistry · 年份：1994 · DOI：10.1016/s0021-9258(17)31601-0 · 被引用次数：61 · 研究领域：Antifungal resistance and susceptibility、Fungal and yeast genetics research、Peptidase Inhibition and Analysis

2977) as a probe.Sequencing of the fulllength gene revealed an open reading frame that can encode a protein of 699 amino acids.The deduced NIXzterminal amino acid sequence did not correspond with that determined from the purified secretory acid proteinase; however, the encoded protein is antigenically related to secretory acid proteinase and has a putative active site for acid proteinase.Interestingly, the amino acid sequence of the NHz-terminal 215 residues of Acprp is highly similar to the DNA binding domain of Stel2p of Saccharomyces cerevisiae.Gel retardation experiments showed that this region of Acprp, like Stelap, could bind to S. cerevisiae pheromone response elements, suggesting that Acprp has a function similar to Stel2p.Chimeric constructs composed of S. cereuisiae STEl2 and C. albicans ACPR genes complemented the mating defect of S. cerevisiae a or a stel2 mutants.Our results suggest the presence of a signal transduction system in C. albicans similar to that of S. cerevisiae mating pathway.Among the clinically important Candida species, Candida albicans is the most pathogenic.It is an opportunistic pathogen that causes candidiasis in human beings and other warm blooded animals.It occurs naturally as a diploid and lacks a sexual phase in its life cycle.When grown in a medium containing bovine serum albumin or other proteins as a sole nitrogen source, C. albicans and some other Candida species secrete acid proteinases (Banerjee et al., 1991;Ruchel, 1981;Staib, 1965S...