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 phosphatases

FEBS Letters
M BachmannS C Huber

Abstract

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 site (Ser-543). First, a phosphorylated synthetic peptide based on the regulatory site can prevent and also reverse the inactivation of phospho-NR caused by 14-3-3 proteins. Second, sequence-specific and phosphorylation-dependent binding of the aforementioned synthetic peptide to the 14-3-3 proteins was demonstrated in vitro. Third, 14-3-3 proteins were required for the ATP-dependent phosphorylation of NR (as assessed by activity measurements) in the presence of NR-kinase and leaf protein phosphatases. Lastly, we demonstrate specificity of recombinant Arabidopsis 14-3-3 isoforms in the interaction with phospho-NR: omega> chi> upsilon> phi, psi.

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Citations

Sep 30, 2000·Plant Science : an International Journal of Experimental Plant Biology·K AppenrothC Lillo
Feb 20, 2002·The Plant Journal : for Cell and Molecular Biology·Gurdeep S Athwal, Steven C Huber
Feb 28, 2002·The Plant Journal : for Cell and Molecular Biology·Juqiang YanHong Zhang
Apr 17, 1999·The Plant Journal : for Cell and Molecular Biology·D ToroserS C Huber
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Jan 1, 2003·Journal of Experimental Botany·Sylviane ComparotThomas Martin
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Apr 10, 1999·Plant Physiology·M R Roberts, D J Bowles
Oct 10, 2007·Biochemistry. Biokhimii︠a︡·Yuan YaoJin-Yuan Liu
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Aug 13, 2014·Journal of Experimental Botany·Réjane Pratelli, Guillaume Pilot
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Jun 16, 2007·Biochimica Et Biophysica Acta·Helene L CardasisRobert J Ferl
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Jun 15, 2007·Journal of Biochemistry and Molecular Biology·Yuan YaoJin-Yuan Liu
Sep 27, 2014·The Plant Journal : for Cell and Molecular Biology·Jing GaoAlbertus H de Boer

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