Open AccessRetention of a co‐translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum
Author(s) -
Ramezani Rad Massoud,
Katz Henning
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06380.x
Subject(s) - endoplasmic reticulum , mutant , biochemistry , cleavage (geology) , saccharomyces cerevisiae , chemistry , carboxypeptidase , microsome , protein biosynthesis , secretory pathway , microbiology and biotechnology , golgi apparatus , biology , in vitro , enzyme , yeast , gene , paleontology , fracture (geology)
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. CpY 1 mutant showed retention of core glycosylated material (proCpY 1 ) 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.