A novel mechanism of glutamine synthetase inactivation by ammonium in the cyanobacterium Synechocystis sp. PCC 6803. Involvement of an inactivating protein

FEBS Letters

Florencio, F.J.¹  Reyes, J.C.¹ 

[1] Instituto de Bioquimica Vegetal y Fotosintesis, Universidad de Sevilla-CSIC, Apdo 1113, 41080-Sevilla, Spain

关键词: Glutamine synthetase;    Synechocystis 6803;    Cyanobacteria;    Ammonium assimilation;    Enzyme inactivation;    GS;    glutamine synthetase;    EDC;    1-ethyl-3-(3-dimethylaminopropyl)carbodiimide;    PAGE;    polyacrylamide gel electrophoresis;    SDS sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(95)00544-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The glutamine synthetase of the cyanobacterium Synechocystis sp. PCC 6803 can be inactivated in vivo by ammonium addition by a new mechanism that involves the binding to the enzyme of an inactivating factor. This binding provokes a different mobility of the inactive enzyme with respect to the active form in non-denaturing PAGE, but not in SDS-PAGE. This modification of glutamine synthetase is for the first time visualized by Western blot analysis of the active and inactive forms. Cross-linking experiments using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) demonstrate the existence of two main complexes of 56 kDa and 67 kDa between the inactivating factor and the glutamine synthetase subunit (53 kDa) in the inactive but not in the active form of glutamine synthetase.

【 授权许可】

Unknown