Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic proteases encoded by the YPS3 gene

Abstract

A new aspartic protease from Saccharomyces cerevisiae, with a high degree of similarity with yapsin 1 and yapsin 2 and a specificity for basic residue cleavage sites of prohormones, has been cloned. This enzyme was named yapsin 3. Expression of a C-terminally truncated non-membrane anchored yapsin 3 in yeast yielded a heterogeneous protein between 135-200 kDa which, upon treatment with endoglycosidase H, migrated as a 60 kDa form. Amino-acid analysis of the N-terminus of expressed yapsin 3 revealed two different N-terminal residues, serine-48 and phenylalanine-54, which followed a dibasic and a monobasic residue respectively. Cleavage of several prohormones by non-anchored yapsin 3 revealed a specificity distinct from that of yapsin 1.

Expression Analysis of BACE2 in Brain and Peripheral Tissues

“…(24 -26). Based on this observation, Olsen et al (1999) have proposed that the Yapsins may be involved in the conversion of membrane-bound precursors to secreted proteins. Membrane attachment through the Yapsin GPI anchor may facilitate the processing of membrane-bound precursor proteins by concentrating the enzyme at the lipid bilayer.…”

An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features

“…The S. cerevisiae aspartic proteases yapsin 1, 2 and 3 have all been shown to be GPI-anchored proteins (Ash et al, 1995;Cawley et al, 1995;Komano & Fuller, 1995;Olsen et al, 1999). Recently, rules for fungal GPI modification motifs have been described (Eisenhaber et al, 2004) and an algorithm is available at a website server (fungal BIG-p predictor, http://mendel.imp.univie.ac.at/gpi/fungi/gpi_fungi.html).…”

Yapsins Are a Family of Aspartyl Proteases Required for Cell Wall Integrity in Saccharomyces cerevisiae

“…The founding members of this family, YPS1 and -2 (17,32), were identified as suppressors of null mutations in KEX2, a trans-Golgi network-localized serine protease that processes secretory proteins such as pro-␣-factor and the exoglucanase Exg1p (3,53). The remaining three yapsins were subsequently identified by sequence homology following completion of the S. cerevisiae genome sequence (47). Like Kex2p, three of the yapsins (Yps1p, -2p, and -3p) cleave proteins and peptides C terminal to basic residues, both in vivo and in vitro (8,33).…”