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Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent


Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent



Journal of Cell Biology 105(6 Part 2): 2905-2914



ISSN/ISBN: 0021-9525

PMID: 3320059

DOI: 10.1083/jcb.105.6.2905

In Saccharomyces cerevisiae, nascent carboxypeptidase Y (CPY) is directed into the endoplasmic reticulum by an NH2-terminal signal peptide that is removed before the glycosylated protein is transported to the vacuole. In this paper, we show that this signal peptide does not function in mammalian cells: CPY expressed in COS-1 cells is not glycosylated, does not associate with membranes, and retains its signal peptide. In a mammalian cell-free protein-synthesizing system, CPY is not translocated into microsomes. However, if the CPY signal is either mutated to increase its hydrophobicity or replaced with that of influenza virus hemagglutinin, the resulting precursors are efficiently translocated both in vivo and in vitro. The implications of these results for models of signal sequence function are discussed.

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Accession: 006829115

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