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PMID: 9725832 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor.

Genetics ·Vol. 150 ·No. 1 ·1998-09-00 ·Pages 95-101

Boyartchuk VL, Rine J

Abstract

In eukaryotes small secreted peptides are often proteolytically cleaved from larger precursors. In Saccharomyces cerevisiae multiple proteolytic processing steps are required for production of mature 12-amino-acid a-factor from its 36-amino-acid precursor. This study provides additional genetic data supporting a direct role for Afc1p in cleavage of the carboxyl-terminal tripeptide from the CAAX motif of the prenylated a-factor precursor. In addition, Afc1p had a second role in a-factor processing that was independent of, and in addition to, its role in the carboxyl-terminal processing in vivo. Using ubiquitin-a-factor fusions we confirmed that the pro-region of the a-factor precursor was not required for production of the mature pheromone. However, the pro-region of the a-factor precursor contributed quantitatively to a-factor production.

MeSH Terms
Amino Acids/chemistry Base Sequence DNA Primers Endopeptidases/metabolism Mating Factor Membrane Proteins Metalloendopeptidases/metabolism Peptides/metabolism Proprotein Convertases Protein Precursors/chemistry,metabolism Protein Prenylation Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Substrate Specificity
Chemicals
Amino Acids DNA Primers Membrane Proteins Peptides Protein Precursors Saccharomyces cerevisiae Proteins Mating Factor Endopeptidases Proprotein Convertases RCE1 protein, S cerevisiae Metalloendopeptidases STE24 protein, S cerevisiae
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Boyartchuk V L
Division of Genetics, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Rine J
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Article Info
Journal
Genetics
Abbr.
Genetics
ISSN
0016-6731
Published
1998-09-00
Pages
95-101
Language
English
Region
United States
NLM ID
0374636
PMCID
PMC1460331
Subset
IM
Grants
NIGMS NIH HHS · GM-35827 · United States
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