Publication Information
Tsiatsiani et al., 2013
Abstract
Plant Cell. 2013 Aug;25(8):2831-47. doi: 10.1105/tpc.113.115287. Epub 2013 Aug
20.
The Arabidopsis metacaspase9 degradome.
Tsiatsiani L(1), Timmerman E, De Bock PJ, Vercammen D, Stael S, van de Cotte B,
Staes A, Goethals M, Beunens T, Van Damme P, Gevaert K, Van Breusegem F.
Author information:
(1)Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium.
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
phosphoenolpyruvate carboxykinase 1 (AT4G37870), a key enzyme in
gluconeogenesis, is enhanced upon MC9-dependent proteolysis.
DOI: 10.1105/tpc.113.115287
PMCID: PMC3784583
PMID: 23964026 [Indexed for MEDLINE]
