The Multispanning Membrane Protein Ste24p Catalyzes CAAX Proteolysis and NH2-terminal Processing of the Yeast a-Factor Precursor

Amy Tam, Walter K. Schmidt, Susan Doris Michaelis

Research output: Contribution to journalArticle

Abstract

Saccharomyces cerevisiae Ste24p is a multispanning membrane protein implicated in the CAAX proteolysis step that occurs during biogenesis of the prenylated a-factor mating pheromone. Whether Ste24p acts directly as a CAAX protease or indirectly to activate a downstream protease has not yet been established. In this study, we demonstrate that purified, detergent-solubilized Ste24p directly mediates CAAX proteolysis in a zinc-dependent manner. We also show that Ste24p mediates a separate proteolytic step, the first NH 2-terminal cleavage in a-factor maturation. These results establish that Ste24p functions both as a bona fide COOH-terminal CAAX protease and as an a-factor NH2-terminal protease. Importantly, this study is the first to directly demonstrate that a eukaryotic multispanning membrane protein can possess intrinsic proteolytic activity.

Original languageEnglish (US)
Pages (from-to)46798-46806
Number of pages9
JournalJournal of Biological Chemistry
Volume276
Issue number50
DOIs
StatePublished - Dec 14 2001

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Proteolysis
Yeast
Membrane Proteins
Peptide Hydrolases
Yeasts
Mating Factor
Processing
Pheromones
Detergents
Saccharomyces cerevisiae
Zinc

ASJC Scopus subject areas

  • Biochemistry

Cite this

The Multispanning Membrane Protein Ste24p Catalyzes CAAX Proteolysis and NH2-terminal Processing of the Yeast a-Factor Precursor. / Tam, Amy; Schmidt, Walter K.; Michaelis, Susan Doris.

In: Journal of Biological Chemistry, Vol. 276, No. 50, 14.12.2001, p. 46798-46806.

Research output: Contribution to journalArticle

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