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

FEBS Letters

Huber, Steven C.²  Toroser, Dikran²  Athwal, Gurdeep S.¹ 

[1] Department of Horticultural Science, North Carolina State University, Raleigh, NC 27695-7631, USA;US Department of Agriculture, Agricultural Research Service and Departments of Crop Science and Botany, North Carolina State University, Raleigh, NC 27695-7631, USA

关键词: Sucrose-phosphate synthase;    14-3-3 protein;    Spinach;    Protein:protein interaction;    Surface plasmon resonance;    AICAR;    5-aminoimidazole-4-carboxamide ribonucleoside;    MAbs;    monoclonal antibodies;    RU;    response units;    SPR;    surface plasmon resonance;    SPS;    sucrose-phosphate synthase;    ZMP;    5-aminoimidazole-4-carboxamide ribonucleoside monophosphate;   

DOI  :  10.1016/S0014-5793(98)01048-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown