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Genetics

Title:		Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor
Author(s):		Boyartchuk VL; Rine J;
Address:		"Division of Genetics, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA"
Journal Title:		Genetics
Year:		1998
Volume:		150
Issue:		1
Page Number:		95 - 101
DOI:		10.1093/genetics/150.1.95
ISSN/ISBN:		0016-6731 (Print) 0016-6731 (Linking)
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"
Keywords:		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 Saccharo;
Notes:		"MedlineBoyartchuk, V L Rine, J eng GM-35827/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1998/09/02 Genetics. 1998 Sep; 150(1):95-101. doi: 10.1093/genetics/150.1.95"