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Phosphorylated Nitrate Reductase and 14-3-3 Proteins1
Site of Interaction, Effects of Ions, and Evidence for an AMP-Binding Site on 14-3-3 Proteins

Gurdeep S. Athwal, Joan L. Huber, and Steven C. Huber*

United States Department of Agriculture, Agricultural Research Service, and Departments of Horticultural Science (G.S.A., J.L.H.), Crop Science (S.C.H.), and Botany (S.C.H.), North Carolina State University, Raleigh, North Carolina 27695-7695

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 and threonine residues at the +6 to +8 positions, relative to the known regulatory binding site involving serine-543, are important in the interaction with GF14omega , a recombinant plant 14-3-3. Also shown is that an increase in ionic strength with KCl or inorganic phosphate, known physical effectors of NR activity, directly disrupts the binding of protein and peptide ligands to 14-3-3 proteins. Increased ionic strength attributable to KCl caused a change in conformation of GF14omega , resulting in reduced surface hydrophobicity, as visualized with a fluorescent probe. Similarly, it is shown that the 5' isomer of AMP was specifically able to disrupt the inactive phosphorylated NR:14-3-3 complex. Using the 5'-AMP fluorescent analog trinitrophenyl-AMP, we show that there is a probable AMP-binding site on GF14omega .

1   This work was a cooperative investigation of the U.S. Department of Agriculture-Agricultural Research Service and the North Carolina Agricultural Research Service (Raleigh, NC), and was supported by a grant from the U.S. Department of Agriculture-National Research Initiative (grant no. 93-37305-9231 to J.L.H. and S.C.H.).
*   Corresponding author; e-mail steve_huber{at}ncsu.edu; fax 1-919-856-4598.

Plant Physiol. (1998) 118: 1041-1048
Copyright Clearance Center:   0032-0889/98/118//08
© 1998 American Society of Plant Physiologists




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