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Related Experiment Videos

Modulation of Ras and a-factor function by carboxyl-terminal proteolysis

V L Boyartchuk1, M N Ashby, J Rine

  • 1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Science (New York, N.Y.)
|March 21, 1997
PubMed
Summary
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Researchers identified two genes, RCE1 and AFC1, crucial for processing prenylated proteins in yeast. Deleting both genes halted this essential maturation process, impacting Ras protein function.

Area of Science:

  • Molecular Biology
  • Proteomics
  • Yeast Genetics

Background:

  • Prenylated proteins are essential for cellular functions, with maturation involving carboxyl-terminal processing.
  • This processing is critical for the proper localization and signaling of key proteins like Ras.
  • Understanding the enzymes involved is key to deciphering protein maturation pathways.

Purpose of the Study:

  • To identify the genes responsible for the proteolytic processing of prenylated proteins in Saccharomyces cerevisiae.
  • To elucidate the specific roles of the identified genes, RCE1 and AFC1, in protein maturation.
  • To investigate the functional consequences of impaired prenylated protein processing on cellular signaling.

Main Methods:

  • Gene identification and deletion in Saccharomyces cerevisiae.

Related Experiment Videos

  • Biochemical assays to assess proteolytic processing of prenylated proteins.
  • Analysis of protein localization and signaling pathways, including Ras protein function.

    • Main Results:

    • Two genes, RCE1 and AFC1, were identified as essential for prenylated protein processing.
    • Afc1 functions as a zinc protease involved in yeast a-factor processing.
    • Rce1 is involved in processing both Ras protein and a-factor; its disruption affects Ras localization, signaling, and suppresses specific RAS2 mutations.

    Conclusions:

    • RCE1 and AFC1 are the primary genes responsible for the proteolytic maturation of prenylated proteins in yeast.
    • The identified proteases play distinct yet overlapping roles in processing critical signaling proteins.
    • Impaired processing of prenylated proteins leads to significant defects in cellular localization and signal transduction pathways.