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The DNA fragment the exhibited a coding region for a protein with high amino acid similarity to IMP dehydrogenases was cloned and sequence from Candida albicans. The Candida albicans IMH3 gene was characterized as a 2.9-kilodalton DNA fragment that encoded an IMP dehydrogenase. The gene also conferred resistance to the specific IMP dehydrogenase inhibitor mycophenolic acid in a dose-dependent manner. Furthermore, IMH3 was expressed in equal levels in the hyphal and yeast form of Candida albicans.

Cell phenotype and environmental factors may affect the production of specific secreted aspartyl proteinase (Sap) isoenzymes in Candida albicans. Sap activity has been linked to virulence. Monitoring levels of Sap1, Sap2 and Sap3 production in different strains and different growth conditions revealed that the WO-1 strain is unique in producing Saps in certain conditions. Phenotype switching in this strain and yeast

A SAP1 gene of Candida albicans has SAP4 and CARE2 elements positioned upstream. Aspartyl proteinase is the SAP gene product. Distinctive marking of SAP1 alleles indicates the presence of SAD4 gene. Characterization of the WO-1 strain allele shows a nucleotide corresponding to the CARE2 repetitive element.

Three secreted aspartyl proteinases have been located, as characterized by molecular mass and N-terminal sequences from one strain of Candida albicans (Wo-1) in which a phenotypic switching system is expressed. The mature type of one of three particular proteinase isoenzymes, two of which correlate to SAP 1 and SAP 2 genes, is represented by these three proteins. The signals and functioning included in the change between white and opaque cells can be examined since the three proteinase isoenzymes in C. albicans have been identified and their expression has been noted.

The analysis of one of the universal Leu codons, CTG, from several Candida species has shown that it is connected with strange translational events. The positions specified by the CTG codon containing a nonmodified serine (Ser) in Candida albicans are demonstrated by using mass spectrometry and Edman sequencing of peptides from the secreted aspartyl proteinase isoenzyme (Sap1). Unorthodox tRNAs that acknowledge the CTG codon and that are charged in vitro with serine (Ser) have been also identified.

Demonstrates that positions identified by the CTG codon contain a nonmodified serine in Candida albicans, using mass spectrometry and Edman sequencing of peptides. Leucine codon usage in the secreted aspartyl proteinase isoenzyme; Expected and observed peptide characteristics.