Metabolite regulation of the interaction between Arabidopsis thaliana PII and N-acetyl-l-glutamate kinase.
The metabolic control of the interaction between ArabidopsisN-acetyl-l-glutamate kinase (NAGK) and the PII protein has been studied. Both gel exclusion and affinity chromatography analyses of recombinant, affinity-purified PII (trimeric complex) and NAGK (hexameric complex) showed that NAGK strongly interacted with PII only in the presence of Mg-ATP, and that this process was reversed by 2-oxoglutarate (2-OG). Furthermore, metabolites such as arginine, glutamate, citrate, and oxalacetate also exerted a negative effect on the PII-NAGK complex formation in the presence of Mg-ATP. Using chloroplast protein extracts and PII affinity chromatography, NAGK interacted with PII only in the presence of ATP-Mg(2+), and this process was antagonized by 2-OG. These results reveal a complex metabolic control of the PII interaction with NAGK in the chloroplast stroma of higher plants.
Feria Bourrellier
Ana Belén
AB
Institut de Biotechnologie des Plantes, Centre National de la Recherche Scientifique, Université Paris Sud, Orsay, France.
Ferrario-Méry
Sylvie
S
Vidal
Jean
J
Hodges
Michael
M
D000255:Adenosine Triphosphate / Q000378:metabolism*; D017360:Arabidopsis / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism; D007656:Ketoglutaric Acids / Q000378:metabolism; D008274:Magnesium / Q000378:metabolism*; D051922:PII Nitrogen Regulatory Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D017851:Phosphotransferases (Carboxyl Group Acceptor) / Q000037:antagonists & inhibitors / Q000378:metabolism*
D029681:Arabidopsis Proteins; D007656:Ketoglutaric Acids; D051922:PII Nitrogen Regulatory Proteins; C473074:PII protein, Arabidopsis; D000255:Adenosine Triphosphate; D017851:Phosphotransferases (Carboxyl Group Acceptor); C018721:acetylglutamate kinase; D008274:Magnesium