ArticleThe EMBO journal1994
Isolation and characterization of krp, a dibasic endopeptidase required for cell viability in the fission yeast Schizosaccharomyces pombe.
Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 55 citations in OpenAlex.
- Pheromone Response and Mating Behavior in Fission Yeast.Microbiology and molecular biology reviews : MMBR · 2022Review
- The evolution of peptide mating pheromones in fission yeast.Current genetics · 2019Review
- Asymmetric diversification of mating pheromones in fission yeast.PLoS biology · 2019Article
- Kexin-like endoprotease KexB is required for N-glycan processing, morphogenesis and virulence in Aspergillus fumigatus.Fungal genetics and biology : FG & B · 2015Article
- Phylogenetic analysis of Amphioxus genes of the proprotein convertase family, including aPC6C, a marker of epithelial fusions during embryology.International journal of biological sciences · 2006Article
- Reduced proteolysis of secreted gelatin and Yps1-mediated alpha-factor leader processing in a Pichia pastoris kex2 disruptant.Applied and environmental microbiology · 2005Article
- pdf1, a palmitoyl protein thioesterase 1 Ortholog in Schizosaccharomyces pombe: a yeast model of infantile Batten disease.Eukaryotic cell · 2004Article
- Heterologous expression of the Saccharomyces cerevisiae PGU1 gene in Schizosaccharomyces pombe yields an enzyme with more desirable properties for the food industry.Applied and environmental microbiology · 2003Article
- A single-copy gene encodes Kex1, a serine endoprotease of Pneumocystis jiroveci.Infection and immunity · 2003Article
- Activation of the kexin from Schizosaccharomyces pombe requires internal cleavage of its initially cleaved prosequence.Molecular and cellular biology · 1998Article
- Mutations within the propeptide, the primary cleavage site or the catalytic site, or deletion of C-terminal sequences, prevents secretion of proPC2 from transfected COS-7 cells.The Biochemical journal · 1997Article
- Characterization of a 120-Kilodalton pre-S-binding protein as a candidate duck hepatitis B virus receptor.Journal of virology · 1996Article
- cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
The activation of pro-hormones and many precursor proteins involves cleavage by endopeptidases belonging to the subtilisin-like family of enzymes. Here we describe the isolation and characterization of the first member of this family from the fission yeast Schizosaccharomyces pombe. The enzyme, which has been named krp for KEX2-related protease, is a type I membrane-bound endopeptidase that cleaves substrates after pairs of dibasic residues. It appears to be synthesized as a pre-pro-protein that is likely to undergo processing following translocation into the endoplasmic reticulum. Processing has been characterized in a cell-free translation/translocation system prepared from Xenopus eggs. Krp is N-glycosylated on all five of its potential sites and both the pre-sequence and the pro-sequence are quickly removed following translocation, the latter probably by autocatalytic cleavage. The inhibitor profile of krp broadly reflects the known properties of the eukaryotic subtilisin proteases, while its pH and Ca2+ dependence are consistent with it being active within the secretory pathway. One of its physiological substrates is likely to be the pheromone precursor pro-P-factor, which it is shown to process in an in vitro system, but identification of other substrates is complicated because, unlike other members of this family, krp is essential for cell viability.
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