Processing of precursor proteins by preparations of oviduct microsomes.

Abstract:

:The signal peptidases from both chicken oviduct and dog pancreas microsomes have been detected by a post-translational assay and, in the case of dog microsomes, by a cotranslational assay. This proteolytic activity is not sensitive to a variety of conventional protease inhibitors under the conditions used in these assays. Using a synthetic ester substrate, two additional activities have been observed in oviduct microsomes, but neither appears to correspond to the signal peptidase activity. Using cDNA as a probe for specific mRNAs, it was shown that polysomes, in the process of synthesizing secretory proteins, bind to microsomal membrane vesicles. This binding appears to be dependent on the nature of the translation product (presumably the specific signal peptide) rather than on the mRNA itself. In addition, pretreatment of the membrane vesicles with N-ethyl maleimide prevents the vectorial discharge and processing of several secretory proteins but does not inhibit the binding of their polysomes to membranes.

journal_name

Ann N Y Acad Sci

authors

Thibodeau SN,Walsh KA

doi

10.1111/j.1749-6632.1980.tb47251.x

subject

Has Abstract

pub_date

1980-01-01 00:00:00

pages

180-91

eissn

0077-8923

issn

1749-6632

journal_volume

343

pub_type

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