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The isolated, twenty-three-residue-long, N-terminal region of the glutamine synthetase inactivating factor binds to its target

AutorNeira, J.L.; Florencio, Francisco J.; Muro-Pastor, M. Isabel
Fecha de publicación2017
CitaciónBiophysical Chemistry 228: 1- 9 (2017)
ResumenGlutamine synthetase (GS) catalyzes the ATP-dependent formation of glutamine from glutamate and ammonia. The activity of Synechocystis sp. PCC 6803 GS type I is regulated by protein-protein interactions with a 65-residue-long protein (IF7). IF7 binds initially to GS through residues at its N terminus. In this work, we studied the conformational preferences of the N-terminal region of IF7 (IF7pep, residues Ala7-Ala29), its binding to GS and its functional properties. Isolated IF7pep populated a nascent helix in aqueous solution. IF7pep was bound to GS with an affinity constant of 0.4 μM, and a 1:1 stoichiometry. IF7pep did not inactivate GS, suggesting that there were other IF7 regions important to carry out the inactivating function. Binding of IF7pep to GS was electrostatically-driven and it did not follow a kinetic two-state model.
Identificadoresdoi: 10.1016/j.bpc.2017.05.017
issn: 1873-4200
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