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

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

doi:10.1016/S0014-5793(98)01048-5

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

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

Plant Biology

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	110-114
Number of pages	5
Journal	FEBS Letters
Volume	435
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(98)01048-5
State	Published - Sep 11 1998

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

Online availability

10.1016/S0014-5793(98)01048-5

Library availability

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title = "Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins",

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.",

keywords = "14-3-3 protein, Protein:protein interaction, Spinach, Sucrose-phosphate synthase, Surface plasmon resonance",

author = "Dikran Toroser and Athwal, {Gurdeep S.} and Huber, {Steven C.}",

note = "Funding Information: We are grateful to Dr. Christopher Lombardo for coupling the phosphorylated SPS-229 peptide to the sensor chip and for his assistance with the binding assays. This research represents cooperative investigations of the US Department of Agriculture (USDA), Agricultural Research Service, and the North Carolina Agricultural Research Service and was supported by grants from the US Department of Energy (DE-AI05-91ER20031) and USDA-NRI (93-37305-9231). Mention of a trademark or proprietary product does not constitute a guarantee or warranty of the product by the USDA or the North Carolina Agricultural Research Service and does not imply its approval to the exclusion of other products that might also be suitable.",

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PY - 1998/9/11

Y1 - 1998/9/11

N2 - 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.

AB - 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.

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

Abstract

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