We have determined that prepro-carboxypeptidase Y and a truncated form of pre-invertase can be translocated across the yeast microsomal membrane post-translationally in a homologous in vitro system. The yeast secretory protein prepro-alpha-factor which was previously shown to be an efficient posttranslational translocation substrate is therefore not unique in this regard, but rather the yeast ER protein translocation machinery is generally capable of accepting substrates from a ribosome-free, soluble pool. However, within our detection limits, full-length pre-invertase could not be translocated posttranslationally, but was translocated co-translationally. This indicates that not every fully synthesized pre-protein can use this pathway, presumably because normal or aberrant folding characteristics can interfere with translocation competence.
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1 April 1988
Article|
April 01 1988
Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae.
W Hansen,
W Hansen
Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448.
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P Walter
P Walter
Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448.
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W Hansen
Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448.
P Walter
Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448.
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1988) 106 (4): 1075–1081.
Citation
W Hansen, P Walter; Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae.. J Cell Biol 1 April 1988; 106 (4): 1075–1081. doi: https://doi.org/10.1083/jcb.106.4.1075
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