Isolation and sequence analysis of the orotidine‐5'‐phosphate decarboxylase gene (URA3) of Candida utilis. Comparison with the OMP decarboxylase gene family

Abstract

The URA3 gene of Candida utilis encoding orotidine-5'-phosphate decarboxylase enzyme was isolated by complementation in Escherichia coli pyrF mutation. The deduced amino-acid sequence is highly similar to that of the Ura3 proteins from other yeast and fungal species. An extensive analysis of the family of orotidine-5'-phosphate decarboxylase is shown. The URA3 gene of C. utilis was able to complement functionally the ura3 mutation of Saccharomyces cerevisiae.

Development of an integrative DNA transformation system for the yeast Candida utilis

“…Plasmids pURA-2 and pURA-5, containing the URA3 gene of C. utilis, were isolated from the genomic library by complementation [7]. utilis wild-type strain NRRL Y-1084 was used to obtain the mutant strains.…”

Cloning, characterization and functionality of the orotidine‐5′‐phosphate decarboxylase gene (URA3) of the glycolipid‐producing yeast Candida bombicola

“…The URA3 genes of several yeast species of the subphylum Saccharomycotina were matched together in a multiple alignment, revealing several conserved regions. These regions correspond to the conserved amino acid sequences described by Rodriguez et al (1998). The first degenerate primer pair, ura3For1 and ura3Rev1, was designed on the highly conserved FEDRKFADIG (amino acids 87–96; Figure 2) and GD‐LGQQYR‐V regions (amino acids 206–216) (Francois et al , 2004).…”

Neutral 1,3‐Diindolylureas for Nerve Agent Remediation

“…This time, the highly conserved FEDRKFADIG sequence (amino acids 87–96; Figure 1) was affected (Francois et al , 2004). The central lysine residue is believed to play a key role in enzyme activity and comparison between the URA3 genes of several organisms of different phyla indeed brings the conserved region down to three essential amino acids:–D–K–D–(Kimsey and Kaiser, 1992; Rodriguez et al , 1998). In F4, the AAG codon was changed to ACG, mutating the central lysine to a threonine residue.…”