title: Formation of a complex containing ATP, Mg2+, and spermine. Structural evidence and biological significance.
abstract: The conformation of ATP in the presence of Mg2+ and/or spermine was studied by 31P and 1H NMR, to clarify how polyamines interact with ATP. Spermine predominantly interacted with the beta- and gamma-phosphates of ATP in the presence of Mg2+. A conformational change of the beta- and gamma-phosphate of ATP with spermine could not be observed in the absence of Mg2+ by 31P NMR. It was found by 1H NMR that the conformation of adenosine moiety of ATP was not influenced significantly by spermine. The binding of Mg2+ to ATP was slightly inhibited by spermine and vice versa. The results indicate that the binding sites of Mg2+ and spermine on ATP only partially overlap. The PotA protein, an ATP-dependent enzyme, was used as a model system to study the biological role of the ATP-Mg2+-spermine complex. The ATPase activity of PotA was greatly enhanced by spermine. Double reciprocal plots at several concentrations of spermine as an activator indicate that spermine interacts with ATP, but not with PotA. The activity of protein kinase A was also stimulated about 2-fold by spermine. The results suggest that a ternary complex of ATP-Mg2+-spermine may play an important role in some ATP-dependent reactions in vivo and in the physiological effects of endogenous polyamines.
authors.affiliation: Faculty of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan.
authors.forename: D
authors.initials: D
authors.lastname: Meksuriyen
authors.forename: T
authors.initials: T
authors.lastname: Fukuchi-Shimogori
authors.forename: H
authors.initials: H
authors.lastname: Tomitori
authors.forename: K
authors.initials: K
authors.lastname: Kashiwagi
authors.forename: T
authors.initials: T
authors.lastname: Toida
authors.forename: T
authors.initials: T
authors.lastname: Imanari
authors.forename: G
authors.initials: G
authors.lastname: Kawai
authors.forename: K
authors.initials: K
authors.lastname: Igarashi
mesh_terms: D018528:ATP-Binding Cassette Transporters; D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002352:Carrier Proteins / Q000187:drug effects; D002413:Cations, Divalent; D017868:Cyclic AMP-Dependent Protein Kinases / Q000187:drug effects; D029968:Escherichia coli Proteins; D008274:Magnesium / Q000737:chemistry* / Q000378:metabolism; D008565:Membrane Proteins / Q000187:drug effects; D008968:Molecular Conformation; D019906:Nuclear Magnetic Resonance, Biomolecular; D010759:Phosphorus Isotopes; D013096:Spermine / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology
chemical_list: D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins; D002413:Cations, Divalent; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D010759:Phosphorus Isotopes; C096374:PotA protein, E coli; D013096:Spermine; D000255:Adenosine Triphosphate; D017868:Cyclic AMP-Dependent Protein Kinases; D008274:Magnesium