Artículo
A conserved C-terminal peptide of sorghum phosphoenolpyruvate carboxylase promotes its proteolysis, which is prevented by Glc-6P or the phosphorylation state of the enzyme
Autor/es | Gandullo Tovar, Jacinto Manuel
Álvarez Morales, Rosario Feria Bourrellier, Ana Belén Monreal Hermoso, José Antonio Díaz, Isabel Vidal, Jean Echevarría Ruiz de Vargas, Cristina |
Departamento | Universidad de Sevilla. Departamento de Biología Vegetal y Ecología |
Fecha de publicación | 2021 |
Fecha de depósito | 2021-09-06 |
Publicado en |
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Premios | Premio Mensual Publicación Científica Destacada de la US. Facultad de Biología |
Resumen | Main conclusion: A synthetic peptide from the C-terminal end of C4-phosphoenolpyruvate carboxylase is implicated in the proteolysis of the enzyme, and Glc-6P or phosphorylation of the enzyme modulate this effect. Abstract: ... Main conclusion: A synthetic peptide from the C-terminal end of C4-phosphoenolpyruvate carboxylase is implicated in the proteolysis of the enzyme, and Glc-6P or phosphorylation of the enzyme modulate this effect. Abstract: Phosphoenolpyruvate carboxylase (PEPC) is a cytosolic, homotetrameric enzyme that performs a variety of functions in plants. Among them, it is primarily responsible for CO2 fixation in the C4 photosynthesis pathway (C4-PEPC). Here we show that proteolysis of C4-PEPC by cathepsin proteases present in a semi-purified PEPC fraction was enhanced by the presence of a synthetic peptide containing the last 19 amino acids from the C-terminal end of the PEPC subunit (pC19). Threonine (Thr)944 and Thr948 in the peptide are important requirements for the pC19 effect. C4-PEPC proteolysis in the presence of pC19 was prevented by the PEPC allosteric effector glucose 6-phosphate (Glc-6P) and by phosphorylation of the enzyme. The role of these elements in the regulation of PEPC proteolysis is discussed in relation to the physiological context. |
Identificador del proyecto | BFU2007-61431-BMC
AGL2012-35708 AGL2016-75413-P P06-CVI-02186 P12-FQM-489 |
Cita | Gandullo Tovar, J.M., Álvarez Morales, R., Feria Bourrellier, A.B., Monreal Hermoso, J.A., Díaz, I., Vidal, J. y Echevarría Ruiz de Vargas, C. (2021). A conserved C-terminal peptide of sorghum phosphoenolpyruvate carboxylase promotes its proteolysis, which is prevented by Glc-6P or the phosphorylation state of the enzyme. Planta, 254 (3), 43. |
Ficheros | Tamaño | Formato | Ver | Descripción |
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A conserved C‑terminal peptide.pdf | 2.019Mb | [PDF] | Ver/ | |