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

FEBS Letters

Huber, Joan L¹  Winter, Heike¹  Huber, Steven C¹ 

[1] U.S. Department of Agriculture, Agricultural Research Service, Raleigh, NC, USA

关键词: Protein phosphorylation;    Sucrose synthase;    Surface hydrophobicity;    Membrane association;    Gravity response;    Zea mays L. pulvinus;    ANS;    1-anilinonaphthalene-8-sulfonic acid;    bis-ANS;    4;    4′-dianilino-1;    1′-binaphthyl-5;    5′-disulfonic acid;    AP5A;    P1;    P5-di(adenosine-5′)pentaphosphate;    PKA;    catalytic subunit of cAMP-activated protein kinase;    PMSF;    phenylmethylsulfonyl fluoride;    PP;    phosphatase;    Suc;    Sucrose;    SuSy;    sucrose synthase;   

DOI  :  10.1016/S0014-5793(97)01506-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown