| Title: | The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin |
| Author(s): | MacKay VL; Welch SK; Insley MY; Manney TR; Holly J; Saari GC; Parker ML; |
| Address: | "ZymoGenetics, Inc., Seattle, WA 98103" |
| ISSN/ISBN: | 0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking) |
| Abstract: | "Saccharomyces cerevisiae a cells secrete an extracellular protein, called 'barrier' activity, that acts as an antagonist of alpha factor, the peptide mating pheromone produced by mating-type alpha cells. We report here the DNA sequence of BAR1, the structural gene for barrier activity. The deduced primary translation product of 587 amino acids has a putative signal peptide, nine potential asparagine-linked glycosylation sites, and marked sequence similarity of the first two-thirds of the protein with pepsin-like proteases. Barrier activity was abolished by in vitro mutation of an aspartic acid predicted from this sequence homology to be in the active site. Therefore, barrier protein is probably a protease that cleaves alpha factor. The sequence similarity suggests that the first two-thirds of the barrier protein is organized into two distinct structural domains like those of the pepsin-like proteases. However, the BAR1 gene product has a third carboxyl-terminal domain of unknown function; deletion of at least 166 of the 191 amino acids of this region has no significant effect on barrier activity" |
| Keywords: | "Amino Acid Sequence Animals *Aspartic Acid Endopeptidases Base Sequence Cloning, Molecular Endopeptidases/*genetics/metabolism Fungal Proteins/*genetics/metabolism *Genes *Genes, Fungal *Genes, Mating Type, Fungal Molecular Sequence Data Mutation Pepsin A;" |
| Notes: | "MedlineMacKay, V L Welch, S K Insley, M Y Manney, T R Holly, J Saari, G C Parker, M L eng Comparative Study Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1988/01/01 Proc Natl Acad Sci U S A. 1988 Jan; 85(1):55-9. doi: 10.1073/pnas.85.1.55" |
