Post-translational regulation of cytosolic glutamine synthetase of Medicago truncatula

• Tipo: Artigo em Revista Científica Internacional
• Data: 2006

Autores

lima, l (Autor) Outra; seabra, a (Autor) Outra; melo, p (Autor) FCUP; cullimore, j (Autor) Outra; carvalho, h (Autor) REIT

Revista

Título: Journal of Experimental Botany

Vol. 57

Páginas: 2751-2761

ISSN: 0022-0957

Editora: Oxford University Press

Indexação

ISI Web of Knowledge - 54 Citações

Scopus - 62 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-004-J6M

DOI: 10.1093/jxb/erl036

Abstract (EN): It was reported recently that the plastid-located glutamine synthetase (GS2) from Medicago truncatula is regulated by phosphorylation catalysed by a calcium-dependent protein kinase and 14-3-3 interaction. Here it is shown that the two cytosolic GS isoenzymes, GS1a and GS1b, are also regulated by phosphorylation but, in contrast to GS2, GS1 phosphorylation is catalysed by calcium-independent kinase(s) and the phosphorylated enzymes fail to interact with 14-3-3s. Phosphorylation of GS1a occurs at more than one residue and was found to increase the affinity of the enzyme for the substrate glutamate. In vitro phosphorylation assays were used to compare the activity of GS kinase, present in different plant organs, against the three M. truncatula GS isoenzymes. All three GS proteins were phosphorylated by kinases present in leaves, roots, and nodules, but to different extents, suggesting a differential regulation under different metabolic contexts. Cytosolic GS phosphorylation was found to be affected by light in leaves and by active nitrogen fixation in root nodules, whereas GS2 phosphorylation was unaffected by these conditions. Some putative GS-binding phosphoproteins were identified showing both isoenzyme and organ specificity. Two phosphoproteins of 70 and 72 kDa were specifically bound to the cytosolic GS isoenzymes. Interestingly, phosphorylation of these proteins was also influenced by the nitrogen-fixing status of the nodule, suggesting that their phosphorylation and/or binding to GS are related to nitrogen fixation. Taken together, the results presented indicate that GS phosphorylation is modulated by nitrogen fixation in root nodules; these findings open up new possibilities to explore the involvement of this post-translational mechanism in nodule functioning.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 11