tailieunhanh - Báo cáo khoa học: Studies of the ATPase activity of the ABC protein SUR1

The ATP-sensitive potassium (KATP) channel couples glucose metabolism to insulin secretion in pancreatic b-cells. It comprises regulatory sulfonyl-urea receptor 1 and pore-forming subunits. Binding and⁄or hydro-lysis of Mg-nucleotides at the nucleotide-binding domains of sulfonylurea receptor 1 stimulates channel opening and leads to membrane hyperpolari-zation and inhibition of insulin secretion. | ễFEBS Journal Studies of the ATPase activity of the ABC protein SUR1 Heidi de Wet1 Michael V. Mikhailov1 Constantina Fotinou1 Mathias Dreger1 Tim J. Craig1 Catherine Venien-Bryan2 and Frances M. Ashcroft1 1 Henry Wellcome Centre for Gene Function Department of Physiology Anatomy and Genetics University of Oxford UK 2 Laboratory of Molecular Biophysics Department of Biochemistry University of Oxford UK Keywords ABCC8 ATPase activity KATP channel nucleotide-binding domain sulfonylurea receptor Correspondence F. M. Ashcroft University Laboratory of Physiology Parks Road Oxford OX1 3PT UK Fax 44 1865 285812 Tel 44 1865 285810 E-mail Received 4 April2007 revised 8 May 2007 accepted 14 May 2007 doi The ATP-sensitive potassium KATP channel couples glucose metabolism to insulin secretion in pancreatic b-cells. It comprises regulatory sulfonylurea receptor 1 and pore-forming subunits. Binding and or hydrolysis of Mg-nucleotides at the nucleotide-binding domains of sulfonylurea receptor 1 stimulates channel opening and leads to membrane hyperpolarization and inhibition of insulin secretion. We report here the first purification and functional characterization of sulfonylurea receptor 1. We also compared the ATPase activity of sulfonylurea receptor 1 with that of the isolated nucleotide-binding domains fused to maltose-binding protein to improve solubility . Electron microscopy showed that nucleotide-binding domains purified as ring-like complexes corresponding to 8 momomers. The ATPase activities expressed as maximal turnover rate in nmol Pi-s-1 nmol protein -1 were and for sulfonylurea receptor 1 nucleotide-binding domain 1 nucleotide-binding domain 2 and a mixture of nucleotide-binding domain 1 and nucleotide-binding domain 2 respectively. Corresponding Km values in mM were and respectively. Thus sulfonylurea receptor 1 has a lower Km than either of the isolated

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