Phosphoenolpyruvate carboxylase (PEPC) and PEPC-kinase (PEPC-k) isoenzymes in Arabidopsis thaliana: role in control and abiotic stress conditions.
Arabidopsis ppc3 mutant has a growth-arrest phenotype and is affected in phosphate- and salt-stress responses, showing that this protein is crucial under control or stress conditions. Phosphoenolpyruvate carboxylase (PEPC) and its dedicated kinase (PEPC-k) are ubiquitous plant proteins implicated in many physiological processes. This work investigates specific roles for the three plant-type PEPC (PTPC) and the two PEPC-k isoenzymes in Arabidopsis thaliana. The lack of any of the PEPC isoenzymes reduced growth parameters under optimal growth conditions. PEPC activity was decreased in shoots and roots of ppc2 and ppc3 mutants, respectively. Phosphate starvation increased the expression of all PTPC and PPCK genes in shoots, but only PPC3 and PPCK2 in roots. The absence of any of these two proteins was not compensated by other isoforms in roots. The effect of salt stress on PTPC and PPCK expression was modest in shoots, but PPC3 was markedly increased in roots. Interestingly, both stresses decreased root growth in each of the mutants except for ppc3. This mutant had a stressed phenotype in control conditions (reduced root growth and high level of stress molecular markers), but was unaffected in their response to high salinity. Salt stress increased PEPC activity, its phosphorylation state, and L-malate content in roots, all these responses were abolished in the ppc3 mutant. Our results highlight the importance of the PPC3 isoenzyme for the normal development of plants and for root responses to stress.
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Ana B
AB
Feria
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Nadja
N
Bosch
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Alfonso
A
Sánchez
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Ana I
AI
Nieto-Ingelmo
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Clara
C
de la Osa
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Cristina
C
Echevarría
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Sofía
S
García-Mauriño
Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain. monreal@us.es.
Jose Antonio
JA
Monreal
D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism; D015153:Blotting, Western; D018507:Gene Expression Regulation, Developmental; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D010710:Phosphates / Q000378:metabolism; D010730:Phosphoenolpyruvate Carboxylase / Q000235:genetics* / Q000378:metabolism; D018517:Plant Roots / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D018520:Plant Shoots / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D054712:Salinity; D013312:Stress, Physiological
D029681:Arabidopsis Proteins; D007527:Isoenzymes; D010710:Phosphates; C069767:phosphoenolpyruvate carboxylase kinase; D017346:Protein Serine-Threonine Kinases; D010730:Phosphoenolpyruvate Carboxylase
Anaplerotic function; Phosphate starvation; Protein kinase; Salt stress