Proteases and caspase-like activity in the yeast Saccharomyces cerevisiae.
Biochemical Society Transactions
A variety of proteases have been implicated in yeast PCD (programmed cell death) including the metacaspase Mca1 and the separase Esp1, the HtrA-like serine protease Nma111, the cathepsin-like serine carboxypeptideases and a range of vacuolar proteases. Proteasomal activity is also shown to have an important role in determining cell fate, with both pro- and anti-apoptotic roles. Caspase 3-, 6- and 8-like activities are detected upon stimulation of yeast PCD, but not all of this activity is associated with Mca1, implicating other proteases with caspase-like activity in the yeast cell death response. Global proteolytic events that accompany PCD are discussed alongside a consideration of the conservation of the death-related degradome (both at the level of substrate choice and cleavage site). The importance of both gain-of-function changes in the degradome as well as loss-of-function changes are highlighted. Better understanding of both death-related proteases and their substrates may facilitate the design of future antifungal drugs or the manipulation of industrial yeasts for commercial exploitation.
addresses: Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter EX4 4QD, UK.
types: Journal Article; Research Support, Non-U.S. Gov't; Review
Author's post-print version
The final version of record is available at http://www.biochemsoctrans.org/bst/039/bst0391502.htm
© The Authors Journal compilation © 2011 Biochemical Society
Biochemical Society Transactions, 2011, Vol. 39, Issue 5, pp. 1502 - 1508
Place of publication