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Institute/Center: CSIC - Instituto de Bioquímica Vegetal y Fotosíntesis (IBVF)
Author: Lorena Saelices, Rocío Robles-Rengel, Francisco J. Florencio y M. Isabel Muro-Pastor
In cyanobacteria, a reversible process that involves protein-protein interaction with two proteins, the inactivating factors IF7 and IF17, regulates GS. Analysis of these proteins, by a site-directed mutagenesis approach, together with structural data, indicates that a core of three residues (E419, N456 and R459) from GS is essential for the inactivation process. The three residues belong to the last 56 amino acids of the C-terminus of GS. In addition, we have identified three conserved arginine residues of IF7 and IF17 that are essential for the interaction of these proteins with GS. All these residues map in the homologous region of IFs.