title: Minor structural consequences of alternative CUG codon usage (Ser for Leu) in Candida albicans exoglucanase.
abstract: In some species of Candida the CUG codon is encoded as serine and not leucine. In the case of the exo-beta-1,3-glucanase from the pathogenic fungus C. albicans there are two such translational events, one in the prepro-leader sequence and the other at residue 64. Overexpression of active mature enzyme in a yeast host indicated that these two positions are tolerant to substitution. By comparing the crystal structure of the recombinant protein with that of the native (presented here), it is seen how either serine or leucine can be accommodated at position 64. Examination of the relatively few solved protein structures from C. albicans indicates that other CUG encoded serines are also found at non-essential surface sites. However such codon usage is rare in C. albicans, in contrast to C. rugosa, with direct implications for respective recombinant protein production.
authors: Biochemistry Department, School of Medical Sciences, University of Otago, PO Box 56, Dunedin, New Zealand. john.cutfield@stonebow.otago.ac.nz
authors: J F
authors: JF
authors: Cutfield
authors: P A
authors: PA
authors: Sullivan
authors: S M
authors: SM
authors: Cutfield
mesh_terms: D019943:Amino Acid Substitution; D002176:Candida albicans / Q000201:enzymology* / Q000235:genetics; D003062:Codon / Q000235:genetics*; D018360:Crystallography, X-Ray; D004271:DNA, Fungal; D005656:Fungal Proteins / Q000737:chemistry; D043326:Glucan 1,3-beta-Glucosidase; D008958:Models, Molecular; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis / Q000235:genetics*; D011487:Protein Conformation; D001617:beta-Glucosidase / Q000737:chemistry / Q000235:genetics*
chemical_list: D003062:Codon; D004271:DNA, Fungal; D005656:Fungal Proteins; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase