Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation

Sucrose synthase (SuSy) plays an important role in sucrose degradation and occurs both as a soluble and as a membrane-associated enzyme in higher plants. We show that membrane association can vary in vivo in response to gravistimulation, apparently involving SuSy dephosphorylation, and is a reversib...

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Bibliographic Details
Published in:FEBS letters 1997-12, Vol.420 (2-3), p.151-155
Main Authors: Winter, Heike, Huber, Joan L, Huber, Steven C
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Anilino Naphthalenesulfonates - metabolism
ANS, 1-anilinonaphthalene-8-sulfonic acid
AP5A, P1,P5-di(adenosine-5′)pentaphosphate
bis-ANS, 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid
Blotting, Western
Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors
Cyclic AMP-Dependent Protein Kinases - metabolism
Electrophoresis, Polyacrylamide Gel
Enzyme Inhibitors - pharmacology
Fluorescent Dyes - metabolism
Glucosyltransferases - analysis
Glucosyltransferases - metabolism
Gravitation
Gravity response
Life Sciences (General)
Membrane association
Membrane Proteins - metabolism
Phosphorylation
PKA, catalytic subunit of cAMP-activated protein kinase
Plant Proteins - metabolism
PMSF, phenylmethylsulfonyl fluoride
PP, phosphatase
Precipitin Tests
Protein phosphorylation
Solubility
Space life sciences
Suc, Sucrose
Sucrose synthase
Surface hydrophobicity
SuSy, sucrose synthase
Uridine Diphosphate Glucose - metabolism
Zea mays - enzymology
Zea mays L. pulvinus
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Summary:Sucrose synthase (SuSy) plays an important role in sucrose degradation and occurs both as a soluble and as a membrane-associated enzyme in higher plants. We show that membrane association can vary in vivo in response to gravistimulation, apparently involving SuSy dephosphorylation, and is a reversible process in vitro. Phosphorylation of SuSy has little effect on its activity but decreases its surface hydrophobicity as reported with the fluorescent probe bis-ANS. We postulate that phosphorylation of SuSy (and perhaps other membrane proteins) is involved in the release of the membrane-bound enzyme in part as a result of decreased surface hydrophobicity.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01506-8