Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Prohormone processing by yeast proteases.

Y Bourbonnais1, D Germain, L Latchinian-Sadek

  • 1Eukaryotic Genetics Group, National Research Council of Canada, Montréal, Que.

Enzyme
|January 1, 1991
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Black Hole Spectroscopy and Tests of General Relativity with GW250114.

Physical review letters·2026
Same author

GW250114: Testing Hawking's Area Law and the Kerr Nature of Black Holes.

Physical review letters·2025
Same author

Frequency-Dependent Squeezed Vacuum Source for the Advanced Virgo Gravitational-Wave Detector.

Physical review letters·2023
Same author

Selected mitochondrial DNA landscapes activate the SIRT3 axis of the UPR<sup>mt</sup> to promote metastasis.

Oncogene·2017
Same author

Involvement of the BCL2 Gene in 131 Cases of Non-Hodgkin's B Lymphomas: Analysis of Correlations with Immunological Findings and Cell Cycle.

Leukemia & lymphoma·2016
Same author

Sirtuins and the Estrogen Receptor as Regulators of the Mammalian Mitochondrial UPR in Cancer and Aging.

Advances in cancer research·2016
Same journal

More on effects of storage time and temperature on urinary enzymes: a 1-year study.

Enzyme·1992
Same journal

Automated measurement of lactate dehydrogenase, alkaline phosphatase and gamma-glutamyltransferase in urines: an alternative to the manual procedure.

Enzyme·1992
Same journal

Hepatocyte heterogeneity in the metabolism of fatty acids: discrepancies on zonation of acetyl-CoA carboxylase.

Enzyme·1992
Same journal

Characterization of multiple forms of carbonyl reductase from chicken liver.

Enzyme·1992
Same journal

Identification of tyrosylprotein sulfotransferase in rat gastric mucosa.

Enzyme·1992
Same journal

Essential fructosuria: increased levels of fructose 3-phosphate in erythrocytes.

Enzyme·1992
See all related articles

Yeast proteases Kex1p and Kex2p process alpha-pheromone and killer toxin precursors. This study characterizes these enzymes and a novel protease that cleaves at monobasic sites, offering insights into prohormone processing.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Yeast Genetics

Background:

  • The yeast Saccharomyces cerevisiae processes precursor proteins like alpha-pheromone and killer toxin.
  • This processing is mediated by specific proteases, including those encoded by KEX1 and KEX2 genes.

Purpose of the Study:

  • To investigate the Kex1p and Kex2p proteases involved in yeast protein processing.
  • To characterize a novel protease responsible for cleavage at monobasic sites.
  • To explore the utility of yeast as a model for mammalian prohormone processing.

Main Methods:

  • Gene identification and characterization (KEX1, KEX2).
  • Enzyme analysis, including cellular localization and post-translational modification studies.
  • Isolation and characterization of mutants defective in monobasic site processing.

Related Experiment Videos

Main Results:

  • Kex1p and Kex2p proteases are confirmed to process yeast protein precursors.
  • Yeast exhibits processing capabilities at both dibasic and monobasic sites.
  • A novel monobasic-specific protease activity was identified and characterized.
  • Mutants with defects in monobasic processing were successfully isolated.

Conclusions:

  • The yeast Saccharomyces cerevisiae possesses sophisticated protease systems for protein maturation.
  • The identified Kex1p, Kex2p, and monobasic-specific proteases are crucial for processing various yeast proteins.
  • The yeast system serves as a valuable model for understanding conserved prohormone processing mechanisms in higher eukaryotes.