| Title: | Modulation of Ras and a-factor function by carboxyl-terminal proteolysis |
| Author(s): | Boyartchuk VL; Ashby MN; Rine J; |
| Address: | "Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA" |
| DOI: | 10.1126/science.275.5307.1796 |
| ISSN/ISBN: | 0036-8075 (Print) 0036-8075 (Linking) |
| Abstract: | "Prenylated proteins contain a covalently linked cholesterol intermediate near their carboxyl-termini. Maturation of most prenylated proteins involves proteolytic removal of the last three amino acids. Two genes in Saccharomyces cerevisiae, RCE1 and AFC1, were identified that appear to be responsible for this processing. The Afc1 protein is a zinc protease that participates in the processing of yeast a-factor mating pheromone. The Rce1 protein contributes to the processing of both Ras protein and a-factor. Deletion of both AFC1 and RCE1 resulted in the loss of proteolytic processing of prenylated proteins. Disruption of RCE1 led to defects in Ras localization and signaling and suppressed the activated phenotype associated with the allele RAS2val19" |
| Keywords: | "Cell Membrane/metabolism Endopeptidases/chemistry/genetics/*metabolism Fungal Proteins/*metabolism Genes, Fungal Genes, ras Lipoproteins/*metabolism *Membrane Proteins Metalloendopeptidases/chemistry/genetics/*metabolism Mutation Pheromones Proprotein Con;" |
| Notes: | "MedlineBoyartchuk, V L Ashby, M N Rine, J eng GM35827/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1997/03/21 Science. 1997 Mar 21; 275(5307):1796-800. doi: 10.1126/science.275.5307.1796" |
