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FEBS Lett. 1998 Sep 11;435(1):110-4.

Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins.

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US Department of Agriculture, Agricultural Research Service and Department of Crop Science, North Carolina State University, Raleigh 27695-7631, USA.
NC St U, Raleigh


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 and co-immunoprecipitation. The content of 14-3-3s associated with an SPS immunoprecipitate was inversely related to activity, and was specifically reduced when tissue was pretreated with 5-aminoimidazole-4-carboxamide riboside, suggesting metabolite control in vivo. A synthetic phosphopeptide based on Ser-229 was shown by surface plasmon resonance to bind a recombinant plant 14-3-3, and addition of the phosphorylated SPS-229 peptide was found to stimulate the SPS activity of an SPS:14-3-3 complex. Taken together, the results suggest a regulatory interaction of 14-3-3 proteins with Ser-229 of SPS.

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