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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.
Asunto(s)

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

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