ArticleMolecular and cellular biology2000
The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Comprehensive analysis of CXXX sequence space reveals that Saccharomyces cerevisiae GGTase-I mainly relies on a2X substrate determinants.G3 (Bethesda, Md.) · 2024Article
- Comprehensive analysis of CXXX sequence space reveals thatbioRxiv : the preprint server for biology · 2024Article
- Extending the reach of homology by using successive computational filters to find yeast pheromone genes.Current biology : CB · 2023Article
- Functional classification and validation of yeast prenylation motifs using machine learning and genetic reporters.PloS one · 2022Article
- Article
- Ste24: An Integral Membrane Protein Zinc Metalloprotease with Provocative Structure and Emergent Biology.Journal of molecular biology · 2020Review
- The tripartite architecture of the eukaryotic integral membrane protein zinc metalloprotease Ste24.Proteins · 2020Article
- Protein Farnesyltransferase Catalyzes Unanticipated Farnesylation and Geranylgeranylation of Shortened Target Sequences.Biochemistry · 2020Article
- Protein Prenylation in Plant Stress Responses.Molecules (Basel, Switzerland) · 2019Review
- Rce1: mechanism and inhibition.Critical reviews in biochemistry and molecular biology · 2018Review
- a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed and Retain Wild-Type Bioactivity.Bioconjugate chemistry · 2018Article
- A shunt pathway limits the CaaX processing of Hsp40 Ydj1p and regulates Ydj1p-dependent phenotypes.eLife · 2016Article
- Ste24p Mediates Proteolysis of Both Isoprenylated and Non-prenylated Oligopeptides.The Journal of biological chemistry · 2016Article
- Towards the systematic mapping and engineering of the protein prenylation machinery in Saccharomyces cerevisiae.PloS one · 2015Article
- A combination of metabolic labeling and 2D-DIGE analysis in response to a farnesyltransferase inhibitor facilitates the discovery of new prenylated proteins.Molecular bioSystems · 2014Article
- Article
- Structure of the integral membrane protein CAAX protease Ste24p.Science (New York, N.Y.) · 2013Article
- Characterization of a novel microcin that kills enterohemorrhagic Escherichia coli O157:H7 and O26.Applied and environmental microbiology · 2012Article
- Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.Microbiology and molecular biology reviews : MMBR · 2012Review
- Type-I prenyl protease function is required in the male germline of Drosophila melanogaster.G3 (Bethesda, Md.) · 2012Article
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6 authors.
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Abstract
Many proteins that contain a carboxyl-terminal CaaX sequence motif, including Ras and yeast a-factor, undergo a series of sequential posttranslational processing steps. Following the initial prenylation of the cysteine, the three C-terminal amino acids are proteolytically removed, and the newly formed prenylcysteine is carboxymethylated. The specific amino acids that comprise the CaaX sequence influence whether the protein can be prenylated and proteolyzed. In this study, we evaluated processing of a-factor variants with all possible single amino acid substitutions at either the a(1), the a(2), or the X position of the a-factor Ca(1)a(2)X sequence, CVIA. The substrate specificity of the two known yeast CaaX proteases, Afc1p and Rce1p, was investigated in vivo. Both Afc1p and Rce1p were able to proteolyze a-factor with A, V, L, I, C, or M at the a(1) position, V, L, I, C, or M at the a(2) position, or any amino acid at the X position that was acceptable for prenylation of the cysteine. Eight additional a-factor variants with a(1) substitutions were proteolyzed by Rce1p but not by Afc1p. In contrast, Afc1p was able to proteolyze additional a-factor variants that Rce1p may not be able to proteolyze. In vitro assays indicated that farnesylation was compromised or undetectable for 11 a-factor variants that produced no detectable halo in the wild-type AFC1 RCE1 strain. The isolation of mutations in RCE1 that improved proteolysis of a-factor-CAMQ, indicated that amino acid substitutions E139K, F189L, and Q201R in Rce1p affected its substrate specificity.
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