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

Hormone processing and membrane-bound proteinases in yeast.

T Achstetter, D H Wolf

    The EMBO Journal
    |January 1, 1985
    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

    Common and dissociable regional cerebral blood flow differences associate with dimensions of psychopathology across categorical diagnoses.

    Molecular psychiatry·2017
    Same author

    Prefrontal cortical thinning links to negative symptoms in schizophrenia via the ENIGMA consortium.

    Psychological medicine·2017
    Same author

    Cortical abnormalities in bipolar disorder: an MRI analysis of 6503 individuals from the ENIGMA Bipolar Disorder Working Group.

    Molecular psychiatry·2017
    Same author

    Positive symptoms associate with cortical thinning in the superior temporal gyrus via the ENIGMA Schizophrenia consortium.

    Acta psychiatrica Scandinavica·2017
    Same author

    Subcortical brain volume abnormalities in 2028 individuals with schizophrenia and 2540 healthy controls via the ENIGMA consortium.

    Molecular psychiatry·2015
    Same author

    Connectome-wide network analysis of youth with Psychosis-Spectrum symptoms.

    Molecular psychiatry·2015

    Researchers identified proteinase yscF, a membrane-bound enzyme crucial for processing the alpha-factor pheromone precursor in Saccharomyces cerevisiae. This enzyme specifically cleaves after basic amino acid pairs, aiding in hormone maturation.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Yeast Genetics

    Background:

    • The alpha-factor pheromone in Saccharomyces cerevisiae is synthesized as a precursor protein.
    • Processing of the alpha-factor precursor involves specific proteolytic cleavage events.
    • Understanding these processing enzymes is key to deciphering yeast mating behavior.

    Purpose of the Study:

    • To identify peptidases responsible for processing the alpha-factor precursor protein.
    • To characterize a novel enzyme involved in hormone maturation in yeast.
    • To investigate the role of specific cleavage sites in precursor protein processing.

    Main Methods:

    • Screening for peptidase activity using synthetic model peptides representing alpha-factor precursor cleavage sites.

    Related Experiment Videos

  • Enzyme assays performed on a mutant yeast strain lacking specific vacuolar peptidases.
  • Characterization of enzyme kinetics, substrate specificity, and cofactor dependency.
  • Analysis of enzyme activity in a kex2 mutant defective in alpha-factor precursor processing.

    • Main Results:

    • A membrane-bound enzyme, designated proteinase yscF, was detected using the chromogenic substrate Cbz-Tyr-Lys-Arg-4-nitroanilide.
    • Proteinase yscF specifically cleaves after basic amino acid pairs (Lys-Arg), consistent with a role in alpha-factor processing.
    • Optimum activity at pH 7.2, enhanced by Triton X-100, and dependent on Ca2+ ions.
    • The enzyme is inhibited by EGTA, EDTA, and mercurials, but not phenylmethylsulfonyl fluoride, distinguishing it from trypsin-like proteases.
    • Proteinase yscF activity was absent in the kex2 mutant, which accumulates an unprocessed alpha-factor precursor.

    Conclusions:

    • Proteinase yscF is a novel membrane-bound peptidase involved in the maturation of the alpha-factor pheromone precursor in Saccharomyces cerevisiae.
    • Its specific cleavage after basic amino acid pairs suggests a critical role in the final steps of hormone processing.
    • The absence of activity in kex2 mutants links proteinase yscF directly to the established alpha-factor processing pathway.