Glutamine synthetase inactivation by protein-protein interaction

被引：77

作者：

García-Domínguez, M ^{[1
]}

Reyes, JC ^{[1
]}

Florencio, FJ ^{[1
]}

机构：

[1] Univ Seville, Inst Bioquim Vegetal & Fotosintesis, Ctr Invest Cient Isla de la Cartuja, CSIC, E-41092 Seville, Spain

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 13期

关键词：

nitrogen metabolism; cyanobacteria; Synechocystis; 6803; enzyme regulation;

D O I：

10.1073/pnas.96.13.7161

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Glutamine synthetase (GS; EC 6.3.1.2) is the pivotal enzyme of nitrogen metabolism in prokaryotes. Control of bacterial GS activity by reversible adenylylation has provided one of the classical paradigms of signal transduction by cyclic cascades. By contrast, in the present work we show that cyanobacterial GS is controlled by a different mechanism that involves the interaction of two inhibitory polypeptides with the enzyme. Both inactivating factors (IFs), named IF7 and IF17, are required in vivo for complete GS inactivation. Inactive GS-IF7 and GS IF17 complexes were reconstituted in vitro by using Escherichia coli expressed purified proteins. Our data suggest that control of GS activity is exerted by regulating the levels of IF7 and IF17.

引用

页码：7161 / 7166

页数：6

共 31 条

[1] NOVEL SUBUNIT SUBUNIT INTERACTIONS IN THE STRUCTURE OF GLUTAMINE-SYNTHETASE [J].