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- Title
Arabidopsis METACASPASE9 Degradome.
- Authors
Tsiatsiani, Liana; Timmerman, Evy; Bock, Pieter-Jan De; Vercammen, Dominique; Stael, Simon; van de Cotte, Brigitte; Staes, An; Goethals, Marc; Beunens, Tine; Damme, Petra Van; Gevaert, Kris; Breusegem, Frank Van
- Abstract
Metacaspases are distant relatives of the metazoan caspases, found in plants, fungi, and protists. However, in contrast with caspases, information about the physiological substrates of metacaspases is still scarce. By means of N-terminal combined fractional diagonal chromatography, the physiological substrates of METACASPASE9 (MC9; AT5G04200) were identified in young seedlings of Arabidopsis thaliana on the proteome-wide level, providing additional insight into MC9 cleavage specificity and revealing a previously unknown preference for acidic residues at the substrate prime site position P1′. The functionalities of the identified MC9 substrates hinted at metacaspase functions other than those related to cell death. These results allowed us to resolve the substrate specificity of MC9 in more detail and indicated that the activity of phospho enol pyruvate carboxykinase 1 (AT4G37870), a key enzyme in gluconeogenesis, is enhanced upon MC9-dependent proteolysis.
- Subjects
BIOCHEMICAL substrates; ARABIDOPSIS; CASPASES; CELL death; PROTEOLYSIS
- Publication
Plant Cell, 2013, Vol 25, Issue 8, p2831
- ISSN
1040-4651
- Publication type
Article
- DOI
10.1105/tpc.113.115287