Signal sequence processing in rough microsomes

Item Type:	Article
Title:	Signal sequence processing in rough microsomes
Creators Name:	Lyko, F. and Martoglio, B. and Jungnickel, B. and Rapoport, T.A. and Dobberstein, B.
Abstract:	Secretory proteins are synthesized with a signal sequence that is usually cleaved from the nascent protein during the translocation of the polypeptide chain into the lumen of the endoplasmic reticulum. To determine the fate of a cleaved signal sequence, we used a synchronized in vitro translocation system. We found that the cleaved signal peptide of preprolactin is further processed close to its COOH terminus. The resulting fragment accumulated in the microsomal fraction and with time was released into the cytosol. Signal sequence cleavage and processing could be reproduced with reconstituted vesicles containing Sec61, signal recognition particle receptor, and signal peptidase complex.
Keywords:	Amino Acid Sequence, Cytosol, Kinetics, Microsomes, Molecular Sequence Data, Mutation, Pancreas, Peptide Fragments, Post-Translational Protein Processing, Prolactin, Protein Precursors, Protein Sorting Signals, Animals, Dogs
Source:	Journal of Biological Chemistry
ISSN:	0021-9258
Publisher:	American Society for Biochemistry and Molecular Biology
Volume:	270
Number:	34
Page Range:	19873-19878
Date:	25 August 1995
Official Publication:	https://doi.org/10.1074/jbc.270.34.19873
PubMed:	View item in PubMed

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