Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
Current BiologyPublished 1 September 1996Open access
Greg B. G. Moorhead, Pauline Douglas, Nick Morrice, Marie Scarabel, Alastair Aitken, Carol MacKintosh
Citations255
SJR quartileQ1
SJR score2.71
SNIP1.83
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TL;DR
The findings establish that the mechanism of inactivation of NR involves the phosphorylation of Ser 543 followed by interaction with one or more plant 14-3-3 proteins, and suggest that the phosphoserine259-Raf-1 peptide and fusicoccin may be of general use for disrupting the interaction of 14- 3-3 with its target proteins.
Abstract
Our findings establish that the mechanism of inactivation of NR involves the phosphorylation of Ser 543 followed by interaction with one or more plant 14-3-3 proteins. These results support the idea of a common mechanism for binding of 14-3-3 to its targets in all eukaryotes, and suggest that the phosphoserine259-Raf-1 peptide and fusicoccin may be of general use for disrupting the interaction of 14-3-3 with its target proteins. We propose that the plant plasma-membrane H+-ATPase is regulated in an analogous manner to NR-NIP, and speculate that 14-3-3 proteins provide a link between 'sensing' the activity state of NR and signalling to other cellular processes in plants.
Keywords
Agricultural and Biological SciencesBiochemistry, Genetics and Molecular Biology
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