dc.contributor.author | Wilkinson, D | |
dc.contributor.author | Ramsdale, M | |
dc.date.accessioned | 2013-11-18T10:05:32Z | |
dc.date.issued | 2011-10 | |
dc.description.abstract | 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. | en_GB |
dc.identifier.citation | Biochemical Society Transactions, 2011, Vol. 39, Issue 5, pp. 1502 - 1508 | en_GB |
dc.identifier.doi | 10.1042/BST0391502 | |
dc.identifier.other | BST0391502 | |
dc.identifier.uri | http://hdl.handle.net/10871/13957 | |
dc.language.iso | en | en_GB |
dc.publisher | Portland Press | en_GB |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pubmed/21936842 | en_GB |
dc.relation.url | http://www.biochemsoctrans.org/bst/default.htm | en_GB |
dc.subject | Amino Acid Sequence | en_GB |
dc.subject | Animals | en_GB |
dc.subject | Apoptosis | en_GB |
dc.subject | Caspases | en_GB |
dc.subject | Evolution, Molecular | en_GB |
dc.subject | Humans | en_GB |
dc.subject | Molecular Sequence Data | en_GB |
dc.subject | Peptide Hydrolases | en_GB |
dc.subject | Saccharomyces cerevisiae | en_GB |
dc.subject | Saccharomyces cerevisiae Proteins | en_GB |
dc.subject | Substrate Specificity | en_GB |
dc.title | Proteases and caspase-like activity in the yeast Saccharomyces cerevisiae. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2013-11-18T10:05:32Z | |
exeter.place-of-publication | England | |
dc.description | addresses: Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter EX4 4QD, UK. | en_GB |
dc.description | types: Journal Article; Research Support, Non-U.S. Gov't; Review | en_GB |
dc.description | Author's post-print version | en_GB |
dc.description | The final version of record is available at http://www.biochemsoctrans.org/bst/039/bst0391502.htm | en_GB |
dc.description | © The Authors Journal compilation © 2011 Biochemical Society | en_GB |
dc.identifier.journal | Biochemical Society Transactions | en_GB |