Minor structural consequences of alternative CUG codon usage (Ser for Leu) in Candida albicans exoglucanase

In some species of Candida the CUG codon is encoded as serine and not leucine. In the case of the exo-β-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 i...

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Bibliographic Details
Published in:Protein engineering 2000-10, Vol.13 (10), p.735-738
Main Authors: Cutfield, J.F., Sullivan, P.A., Cutfield, S.M.
Format: Article
Language:English
Subjects:
alternative codon usage
Amino Acid Substitution
beta-Glucosidase - chemistry
beta-Glucosidase - genetics
Candida albicans
Candida albicans - enzymology
Candida albicans - genetics
Candida rugosa
Codon - genetics
crystal structure
Crystallography, X-Ray
DNA, Fungal
exo-1,3-b-glucanase
exo-^b-1,3-glucanase
exoglucanase
Fungal Proteins - chemistry
Glucan 1,3-beta-Glucosidase
leucine
Models, Molecular
Molecular Sequence Data
Protein Biosynthesis - genetics
Protein Conformation
serine
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Summary:In some species of Candida the CUG codon is encoded as serine and not leucine. In the case of the exo-β-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.
ISSN:0269-2139
1741-0126
1460-213X
1741-0134
DOI:10.1093/protein/13.10.735