Phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxylase kinase isoenzymes play an important role in the filling and quality of Arabidopsis thaliana seed.


Journal

Plant physiology and biochemistry : PPB
ISSN: 1873-2690
Titre abrégé: Plant Physiol Biochem
Pays: France
ID NLM: 9882449

Informations de publication

Date de publication:
01 Nov 2022
Historique:
received: 25 04 2022
revised: 25 07 2022
accepted: 15 08 2022
pubmed: 14 9 2022
medline: 30 9 2022
entrez: 13 9 2022
Statut: ppublish

Résumé

Three plant-type phosphoenolpyruvate carboxylase (PPC1 to PPC3) and two phosphoenolpyruvate carboxylase kinase (PPCKs: PPCK1 and 2) genes are present in the Arabidopsis thaliana genome. In seeds, all PPC genes were found to be expressed. Examination of individual ppc mutants showed little reduction of PEPC protein and global activity, with the notable exception of PPC2 which represent the most abundant PEPC in dry seeds. Ppc mutants exhibited moderately lower seed parameters (weight, area, yield, germination kinetics) than wild type. In contrast, ppck1-had much altered (decreased) yield. At the molecular level, ppc3-was found to be significantly deficient in global seed nitrogen (nitrate, amino-acids, and soluble protein pools). Also, N-deficiency was much more marked in ppck1-, which exhibited a tremendous loss of 95% and 90% in nitrate and proteins, respectively. The line ppck2-had accumulated amino-acids but lower levels of soluble proteins. Regarding carboxylic acid pools, Krebs cycle intermediates were found to be diminished in all mutants; this was accompanied by a consistent decrease in ATP. Lipids were stable in ppc mutants, however ppck1-seeds accumulated more lipids while ppck2-seeds showed high level of polyunsaturated fatty acid oleic and linolenic (omega 3). Altogether, the results indicate that the complete PEPC and PPCK family are needed for normal C/N metabolism ratio, growth, development, yield and quality of the seed.

Identifiants

pubmed: 36099810
pii: S0981-9428(22)00374-6
doi: 10.1016/j.plaphy.2022.08.012
pii:
doi:

Substances chimiques

Carboxylic Acids 0
Isoenzymes 0
Lipids 0
Nitrates 0
Adenosine Triphosphate 8L70Q75FXE
phosphoenolpyruvate carboxylase kinase EC 2.7.1.-
Protein Serine-Threonine Kinases EC 2.7.11.1
Phosphoenolpyruvate Carboxylase EC 4.1.1.31
Nitrogen N762921K75

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

70-80

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier Masson SAS.. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Ana B Feria (AB)

Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes Nº 6, 41012, Sevilla, Spain. Electronic address: anabelen@us.es.

Isabel Ruíz-Ballesta (I)

Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes Nº 6, 41012, Sevilla, Spain.

Guillermo Baena (G)

Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes Nº 6, 41012, Sevilla, Spain.

Noemí Ruíz-López (N)

Dpto. de Mejora Genética y Biotecnología, IHSM La Mayora, UMA-CSIC. Av. Louis Pasteur, 49, 29010, Málaga, Spain.

Cristina Echevarría (C)

Departamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes Nº 6, 41012, Sevilla, Spain.

Jean Vidal (J)

Institute of Plant Sciences Paris-Saclay(IPS2), CNRS, INRA, Univ. Paris-Sud, Univ. d'Evry, Univ. Paris-Diderot, Univ. Paris-Saclay, Batiment 630, Rue Noetzlin, 91192, Gif-sur-Yvette cedex, France.

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Classifications MeSH