tailieunhanh - Báo cáo khoa học: Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs

Calmodulin (CaM) is a cytosolic Ca 2+ signal-transducing protein that binds and activates many different cellular enzymes with physiological rele-vance, including the nitric oxide synthase (NOS) isozymes. CaM consists of two globular domains joined by a central linker; each domain contains an EF hand pair. | ềFEBS Journal Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs Donald E. Spratt1 Elena Newman1 Jennifer Mosher1 Dipak K. Ghosh2 John C. Salerno3 and J. G. Guillemette1 1 Department of Chemistry University of Waterloo ON Canada 2 Department of Medicine Duke University and VA MedicalCenter Durham NC USA 3 Biology Department Rensselaer Polytechnic Institute Troy NY USA Keywords activation binding calmodulin nitric oxide nitric oxide synthase Correspondence J. G. Guillemette Department of Chemistry University of Waterloo Waterloo Ontario N2L 3G1 Canada Fax 1 519 746 0435 Tel 1 519 888 4567 ext. 5954 E-mail jguillem@ Received 23 December 2005 revised 10 February 2006 accepted 20 February 2006 doi Calmodulin CaM is a cytosolic Ca2 signal-transducing protein that binds and activates many different cellular enzymes with physiological relevance including the nitric oxide synthase NOS isozymes. CaM consists of two globular domains joined by a central linker each domain contains an EF hand pair. Four different mutant CaM proteins were used to investigate the role of the two CaM EF hand pairs in the binding and activation of the mammalian inducible NOS iNOS and the constitutive NOS cNOS enzymes endothelial NOS eNOS and neuronal NOS nNOS . The role of the CaM EF hand pairs in different aspects of NOS enzymatic function was monitored using three assays that monitor electron transfer within a NOS homodimer. Gel filtration studies were used to determine the effect of Ca2 on the dimerization of iNOS when coexpressed with CaM and the mutant CaM proteins. Gel mobility shift assays were performed to determine binding stoichiometries of CaM proteins to synthetic NOS CaM-binding domain peptides. Our results show that the N-terminal EF hand pair of CaM contains important binding and activating elements for iNOS whereas the N-terminal EF hand pair in conjunction with the central linker region is .

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