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Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteinsWe 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.
Document ID
20040142229
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Toroser, D.
(US Department of Agriculture, North Carolina State University Agricultural Research Service and Department of Crop Science, Raleigh 27695-7631, United States)
Athwal, G. S.
Huber, S. C.
Davies, E.
Date Acquired
August 22, 2013
Publication Date
September 11, 1998
Publication Information
Publication: FEBS letters
Volume: 435
Issue: 1
ISSN: 0014-5793
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Discipline Plant Biology

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