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Related Experiment Videos

Prepro-alpha-factor has a cleavable signal sequence.

M G Waters1, E A Evans, G Blobel

  • 1Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021.

The Journal of Biological Chemistry
|May 5, 1988
PubMed
Summary
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MAT alpha Saccharomyces cerevisiae secretes alpha-factor, a mating pheromone. This study identifies a novel pro-alpha-factor product, revealing signal peptide cleavage and specific oligosaccharide processing in yeast.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Saccharomyces cerevisiae secretes alpha-factor, a peptide mating pheromone.
  • The precursor, prepro-alpha-factor, undergoes translocation and glycosylation in the endoplasmic reticulum.

Purpose of the Study:

  • To investigate the processing and modification of prepro-alpha-factor in yeast.
  • To identify the nature of a translocated, nonglycosylated product.

Main Methods:

  • In vitro translation/translocation system.
  • Amino-terminal radiosequencing.
  • Enzymatic characterization using glucosidase and mannosidase inhibitors.
  • Analysis of yeast secretory mutants (sec18).

Main Results:

Related Experiment Videos

  • Identified a nonglycosylated product as pro-alpha-factor, indicating signal sequence cleavage.
  • Demonstrated that both eukaryotic and prokaryotic signal peptidases can process prepro-alpha-factor.
  • Confirmed in vivo cleavage in yeast secretory mutants.
  • Characterized oligosaccharides on pro-alpha-factor as Man8GlcNAc2 structures.

Conclusions:

  • Prepro-alpha-factor is cleaved by signal peptidase in vitro and in vivo.
  • The processing and oligosaccharide modifications occur in the endoplasmic reticulum.