The Arabidopsis metacaspase9 degradome.
Plant Cell
; 25(8): 2831-47, 2013 Aug.
Article
en En
| MEDLINE
| ID: mdl-23964026
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 phosphoenolpyruvate carboxykinase 1 (AT4G37870), a key enzyme in gluconeogenesis, is enhanced upon MC9-dependent proteolysis.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Arabidopsis
/
Caspasas
/
Proteínas de Arabidopsis
/
Proteolisis
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Plant Cell
Asunto de la revista:
BOTANICA
Año:
2013
Tipo del documento:
Article
País de afiliación:
Bélgica