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Site‐specific regulatory interaction between spinach leaf sucrose‐phosphate synthase and 14‐3‐3 proteins
Author(s) -
Toroser Dikran,
Athwal Gurdeep S.,
Huber Steven C.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01048-5
Subject(s) - spinach , phosphopeptide , chemistry , biochemistry , immunoprecipitation , sucrose phosphate synthase , peptide , phosphate , surface plasmon resonance , size exclusion chromatography , metabolite , recombinant dna , sucrose , enzyme , sucrose synthase , gene , invertase , materials science , nanoparticle , nanotechnology
We report an Mg 2+ ‐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.