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Site‐specific regulatory interaction between spinach leaf sucrose‐phosphate synthase and 14‐3‐3 proteins
We report an Mg2+‐dependent interaction between spinach leaf sucrose‐phosphate synthase (SPS) and endogenous 14‐3‐3 proteins, as evidenced by co‐elution during gel filtration andExpand
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Divalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase.
Binding of 14-3-3 proteins to nitrate reductase phosphorylated on Ser543 (phospho-NR) inhibits activity and is responsible for the inactivation of nitrate reduction that occurs in darkened leaves.Expand
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Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation.
In this report we address two questions regarding the regulation of phosphorylated nitrate reductase (pNR; EC 1.6.6.1) by 14-3-3 proteins. The first concerns the requirement for millimolarExpand
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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‐543 by endogenous protein
Three lines of evidence indicate that the 14‐3‐3 proteins that inactivate the phosphorylated form of spinach leaf NADH:nitrate reductase (NR) bind to the enzyme at the regulatory phosphorylation siteExpand
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Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an amp-binding site on 14-3-3 proteins.
The inactivation of phosphorylated nitrate reductase (NR) by the binding of 14-3-3 proteins is one of a very few unambiguous biological functions for 14-3-3 proteins. We report here that serine andExpand
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Regulation of glutamate dehydrogenase activity by manipulation of nucleotide supply in Daucus carota suspension cultures
The enzyme glutamate dehydrogenase (GDH, EC 1.4.1.2) is ubiquitous in plant species. It is now generally accepted that the primary role of this enzyme is not assimilation of ammonium and it has beenExpand
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Modulation of 14-3-3 protein interactions with target polypeptides by physical and metabolic effectors.
The proteins commonly referred to as 14-3-3s have recently come to prominence in the study of protein:protein interactions, having been shown to act as allosteric or steric regulators and possiblyExpand
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Overexpression of a directed mutant of 14-3-3ω in Arabidopsis leaves affects phosphorylation and protein content of nitrate reductase.
The 14-3-3 family of proteins are highly conserved signaling proteins in eukaryotes that bind to their client proteins, usually through specific phosphorylated target sequences. While the 14-3-3Expand
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Site of Interaction, Effects of Ions, and Evidence for an AMP-Binding Site on 14-3-3 Proteins
The inactivation of phosphorylated nitrate reductase (NR) by the binding of 14-3-3 proteins is one of a very few unambiguous biological functions for 14-3-3 proteins. We report here that serine andExpand
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