FEBS Letters · 1995 · 62 citations · 27 references
Life SciencesGeneticsMolecular BiologyEnzymologyGene ExpressionProtein BiochemistryDisulfide Bond FormationEnzyme DeficienciesProtein DegradationProteolytic EnzymesYeast BiologyYeast GeneticsDisulfide Bond Isomerase ActivityDisulfide Bond IsomerizationEndoplasmic Reticulum BiochemistryProtein Disulfide IsomeraseYeast Gene Expression RegulationYeast Gene FunctionYeast Gene OverexpressionYeast Gene Regulation
MPD1, a yeast gene the overexpression of which suppresses the inviability caused by the loss of protein disulfide isomerase (PDI) was isolated and characterized. The MPD1 gene product retained a single disulfide isomerase active site sequence (APWCGHCK), an N-terminal putative signal sequence, and a C-terminal endoplasmic reticulum (ER) retention signal, and was a novel member of the PDI family. The gene product, identified in yeast extract, contained core size carbohydrates. MPD1 was not essential for growth, but overexpression of the gene suppressed the maturation defect of carboxypeptidase Y caused by PDI1 deletion, indicative of the related function to PDI in the yeast ER.
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