tailieunhanh - báo cáo khoa hoc : The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis

Human guanylate-binding protein 1 (hGBP1) belongs to the superfamily of large, dynamin-related GTPases. The expression of hGBP1 is induced by stimulation with interferons (mainly interferon-c), and it plays a role in dif-ferent cellular responses to inflammatory cytokines, . pathogen defence, control of proliferation, and angiogenesis. | IFEBS Journal The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis Mark Wehner Simone Kunzelmann f and Christian Herrmann Ruhr-Universitat Bochum Physikalische Chemie I - AG Proteininteraktionen Germany Keywords dynamin GTPase guanine cap guanylate-binding protein interferons Correspondence C. Herrmann Ruhr-Universitat Bochum Physikalische Chemie I Universitatsstr. 150 44780 Bochum Germany Fax 49 2343214785 Tel 49 2343224173 E-mail These authors contributed equally to this work fPresent address MRC National institute for Medical Research Division of PhysicalBiochemistry The Ridgeway Mill Hill London NW7 1AA UK Received 19 July 2011 revised 7 October 2011 accepted 27 October 2011 doi Human guanylate-binding protein 1 hGBPl belongs to the superfamily of large dynamin-related GTPases. The expression of hGBP1 is induced by stimulation with interferons mainly interferon-y and it plays a role in different cellular responses to inflammatory cytokines . pathogen defence control of proliferation and angiogenesis. Although other members of the dynamin superfamily show a diversity of cellular functions they share a common GTPase mechanism that relies on nucleotide-controlled oligomerization and self-activation of the GTPase. Previous structural studies on hGBP1 have suggested a mechanism of GTPase and GDPase activity that as a critical step involves dimerization of the large GTP-binding domains. In this study we show that the guanine cap of hGBP1 is the key structural element responsible for dimerization and is thereby essential for selfactivation of the GTPase activity. Studies of concentration-dependent GTP hydrolysis showed that mutations of residues in the guanine cap in particular Arg240 and Arg244 resulted in higher dissociation constants of the dimer whereas the maximum hydrolytic activity was largely unaffected. Additionally we identified an .

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