Ste24 protease

Walter K. Schmidt, Susan Michaelis

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations


This chapter examines the activity, specificity and structural chemistry of ste24protease. The STE24 gene product plays two distinct proteolytic roles in the a-factor biogenesis pathway, one inC-terminal modification and another in N-terminal cleavage. Consistent with its proposed proteolytic functions, Ste24p possesses a consensus HEXXH zinc-metalloprotease motif. A notable feature of Ste24p that sets it apart from most other zinc metalloproteases is that it contains multiple membrane spans. Reconstitution studies in vitro utilizing crude Ste24p-containing membranes have confirmed that active Ste24p is indeed membrane associated and is required for dual roles in -factor processing. The proof for whether Ste24p acts directly as the -factor protease or indirectly to activate a downstream protease has awaited the purification of Ste24p. Ste24p is a 52 kDa integral membrane protein that resides in the membrane of the endoplasmic reticulum, along with two other CaaX-processing components, Rce lp and Ste 14p. Hydropathy analysis predicts that Ste24p may span the ER membrane seven times. Protease protection studies with microsomes containing N- or C-terminally epitope-tagged versions of Ste24p have demonstrated that the N-terminus of Ste24p is luminally disposed while the C-terminus is cytosolically disposed.

Original languageEnglish (US)
Title of host publicationHandbook of Proteolytic Enzymes, Second Edition
Subtitle of host publicationVolume 1: Aspartic and Metallo Peptidases
Number of pages6
ISBN (Electronic)9780120796113
ISBN (Print)9780124121058
StatePublished - Jan 1 2004

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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