Characterization of a gene encoding a Pichia pastoris protein disulfide isomerase.
Protein disulphide isomerases belong to the thioredoxin superfamily of protein-thiol oxidoreductases that have two double-cysteine redox-active sites and take part in protein folding in the endoplasmic reticulum (ER). We report here the cloning of a Pichia pastoris genomic DNA fragment (2919 bp) that encodes the full length of a protein disulphide isomerase (PpPDI). The deduced amino acid sequence of PDI consists of 517 residues and carries the two characteristic PDI-type redox-active domains -CGHC-, separated by 338 residues, and two potential N-glycosylation sites. The N-terminal end forms a putative signal sequence, and an acidic C-terminal region represents a possible calcium-binding domain. Together with the -HDEL ER retrieval sequence at the C-terminus, these features indicate that the gene encodes a redox-active ER-resident protein disulphide isomerase. The nucleotide sequence, which also contains two other open reading frames, has been submitted to the EMBL Nucleotide Sequence Database, Accession No. AJ302014.
Warsame
A
A
Department of Biochemistry, University of Oslo, Oslo, 0316, Norway.
Vad
R
R
Kristensen
T
T
Oyen
T B
TB
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D005800:Genes, Fungal; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010843:Pichia / Q000201:enzymology* / Q000235:genetics*; D019704:Protein Disulfide-Isomerases / Q000235:genetics*; D020506:Untranslated Regions
D020506:Untranslated Regions; D019704:Protein Disulfide-Isomerases