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

Dikran Toroser, Gurdeep S. Athwal, Steven C. Huber

Research output: Contribution to journalArticlepeer-review

Abstract

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. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)110-114
Number of pages5
JournalFEBS Letters
Volume435
Issue number1
DOIs
StatePublished - Sep 11 1998
Externally publishedYes

Keywords

  • 14-3-3 protein
  • Protein:protein interaction
  • Spinach
  • Sucrose-phosphate synthase
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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