Retention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum.
Co-translational translocation of Saccharomyces cerevisiae vacuolar glycoprotein carboxypeptidase Y (CpY) was highly efficient when studied with an in vivo and in vitro homologous system, comparison of limited proteolytic cleavage of immunoprecipitated translational products of CpY and subcellular localisation of a mutant CpY. The efficient segregation of CpY mRNA in highly purified fractions of rough microsomes was characterised. CpY1 mutant showed retention of core glycosylated material (proCpY1) in the rough and smooth endoplasmic reticulum fractions. It is suggested that the presence of structures that are incompatible with intercompartmental transport of vacuolar protein leads to retention of the mutated CpY by the endoplasmic reticulum.
Ramezani Rad
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M
Institute of Microbiology, Heinrich-Heine-University of Düsseldorf, FRG.
Katz
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H
D001693:Biological Transport, Active; D002268:Carboxypeptidases / Q000235:genetics* / Q000378:metabolism; D043402:Cathepsin A; D004721:Endoplasmic Reticulum / Q000201:enzymology; D006031:Glycosylation; D009154:Mutation; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D014617:Vacuoles / Q000201:enzymology
D029701:Saccharomyces cerevisiae Proteins; D002268:Carboxypeptidases; D043402:Cathepsin A; C499283:PRC1 protein, S cerevisiae; C022633:serine carboxypeptidase