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The regulatory phosphorylated serine in full-length nitrate reductase is necessary for optimal binding to a 14-3-3 protein


The regulatory phosphorylated serine in full-length nitrate reductase is necessary for optimal binding to a 14-3-3 protein



Plant Science 170(2): 394-398



ISSN/ISBN: 0168-9452

DOI: 10.1016/j.plantsci.2005.09.004

Surface plasmon resonance studies and activity assays were used to examine the interaction between tobacco nitrate reductase (NR) from transgenic Nicotiana plumbaginifolia lines and the yeast 14-3-3 protein BMH1. Binding of BMH1 to NR was phosphorylation dependent. The 14-3-3 binding of a mutant tobacco NR protein from a transgenic N. plumbaginifolia line (S521D) lacking the conserved phosphorylation site was reduced by 50%, relative to the wild-type.

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Accession: 004484654

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