Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner.
The third multicopy suppressor gene of the PDI1 deletion from Saccharomyces cerevisiae, MPD2, was isolated and characterized. The MPD2 gene encodes a protein with a putative signal sequence, ER retention signal, and a disulfide isomerase active site like sequence. The amino acid sequence around the active site like sequence is ... similar to the thioredoxin-like domains of PDI and PDI related proteins, although the similarity is comparatively low. A delta-pdi1 strain over-producing Mpd2p showed slow growth and was sensitive to 1 mM dithiothreitol. Mpd2p can be detected in wild type cells and is a glycoprotein. Although the MPD2 gene was not essential for growth, overexpression of the gene partially restored the maturation defect of carboxypeptidase Y caused by the PDI1 deletion. Mutagenesis analysis revealed that Mpd2p can compensate for the loss of PDI with its CXXC sequence.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Carboxypeptidases, Cathepsin A, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Genes, Fungal, Genes, Suppressor, Molecular Sequence Data, Multigene Family, Protein Disulfide-Isomerases, Saccharomyces cerevisiae
Amino Acid Sequence, Binding Sites, Carboxypeptidases, Cathepsin A, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Genes, Fungal, Genes, Suppressor, Molecular Sequence Data, Multigene Family, Protein Disulfide-Isomerases, Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
Date: Oct. 29, 1997
PubMed ID: 9367834
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