RETENTION OF A CO-TRANSLATIONAL TRANSLOCATED MUTANT PROTEIN OF CARBOXYPEPTIDASE-Y OF SACCHAROMYCES-CEREVISIAE IN ENDOPLASMIC-RETICULUM

被引：0

作者：

RAD, MR ^{[1
]}

KATZ, H ^{[1
]}

机构：

[1] FREE UNIV BERLIN,DEPT BIOCHEM & MOLEC BIOL,W-1000 BERLIN 33,GERMANY

来源：

FEMS MICROBIOLOGY LETTERS | 1993年 / 111卷 / 2-3期

关键词：

CARBOXYPEPTIDASE-Y; VACUOLAR GLYCOPROTEIN; HOMOLOGOUS CELL-FREE SYSTEM; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM RETENTION; SACCHAROMYCES-CERVISIAE; YEAST;

D O I：

暂无

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 CoTe 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.

引用

页码：165 / 170

页数：6

共 42 条

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