Antibodies to assess phosphorylation of spinach leaf nitrate reductase on serine 543 and its binding to 14-3-3 proteins

Journal of Experimental Botany

Volumn 52, Issue 359, 2001, Pages 1165-1172

  Weiner, H ^a   Kaiser, W M ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

14 3 3 Proteins; Enzyme inhibition; Nitrate reductase; Protein phosphorylation; Protein:protein interactions

Indexed keywords

ANTIBODIES; ENZYME INHIBITION; IMMUNOLOGY; NITRATES;

PHOSPHORYLATION;

PLANTS (BOTANY);

EID: 0034945805     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/52.359.1165     Document Type: Article

References (26)

1. Partial purification and characterization of a calcium-dependent protein kinase and an inhibitor protein required for inactivation of spinach leaf nitrate reductase
2. 14-3-3 Proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-432 by endogenous protein phosphatases
3. Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase
4. Production of phosphorylation state-specific antibodies
5. Inactivation of nitrate reductase involves NR-protein phosphorylation and subsequent 'binding' of an inhibitor protein
6. Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation
7. Correlation between apparent activation state of nitrate reductase (NR), NR hysterisis and degradation of NR protein
8. Nitrate reductase in higher plants: A case study for transduction of environmental stimuli into control of catalytic activity
9. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
10. Characterization of nitrate reductase from light- and dark-exposed leaves
11. Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves
12. Interaction of 14-3-3 with a non-phosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa
13. Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins
14. Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
15. Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion
16. 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
17. A conserved acidic motif in the N-terminal domain of nitrate reductase is necessary for the inactivation of the enzyme in the dark by phosphorylation and 14-3-3 binding
18. Protein phosphorylation analysis by electrospray ionization-mass spectrometry
19. The 14-3-3 proteins
20. Calyculin A induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo
21. Immunological analysis of the phosphorylation state of maize C4-form phosphoenolpyruvate carboxylase with specific antibodies raised against a synthetic phosphorylated peptide
22. Phosphopeptide mapping and phosphoamino acid analysis on cellulose thin-layer plates
23. Antibodies that distinguish between the serine-158 phospho- and dephospho-form of spinach leaf sucrose-phosphate synthase
24. 14-3-3 Proteins control proteolysis of nitrate reductase in spinach leaves
25. Binding to 14-3-3 proteins is not sufficient to inhibit nitrate reductase in spinach leaves