Mapping the ATP binding site in the plasma membrane h+-ATPase from Kluyveromyces lactis


Por: Sampedro J.G., Nájera H., Uribe-Carvajal S., Ruiz-Granados Y.G.

Publicada: 1 nov 2014
Resumen:
The plasma membrane H+-ATPase from Kluyveromyces lactis contains 14 tryptophan residues. Binding a nucleotide or unfolding with Gnd-HCl quenched intrinsic fluorescence by?˜60 % suggesting that in the H+-ATPase-Nucleotide complex there is solvent-mediated collisional quenching of W505 fluorescence. N-bromosuccinimide (NBS) treatment of H+-ATPase modified a single W residue in both native and Gnd-HCl-unfolded H+-ATPase. Denaturing the H+-ATPase with 1 % SDS led to expose six tryptophan residues while requiring 17 NBS/H+-ATPase. The remaining eight tryptophan residues kept buried indicating a highly stable TM domain. Acrylamide generated static quenching of fluorescence; partial in the native enzyme (V?=?0.43 M-1) and complete in the Gnd-HCl-unfolded H+-ATPase (V?=?0.81 M-1). Collisional quenching (K sv) increased from 3.12 to 7.45 M-1 upon H+-ATPase unfolding. W505 fluorescence titration with NBS yielded a molar ratio of 6 NBS/H+-ATPase and quenched?˜?60 % fluorescence. In the recombinant N-domain, the distance between W505 and MantATP was estimated to be 21 Å by FRET. The amino acid residues involved in nucleotide binding were identified by N-domain molecular modelling and docking with ATP. In the N-domain/ATP complex model, the distance between W505 and ATP was 20.5 Å. ATP binding leads to a conformational change in the N-domain of H+-ATPase that exposes W505 to the environment. © 2014 Springer Science+Business Media New York.

Filiaciones:
Sampedro J.G.:
 Departamento de Biofísica, Instituto de Física, Universidad Autónoma, San-Luis-Potosí-SLP, C.P. 78290, Mexico

Nájera H.:
 Departamento de Ciencias Naturales, Universidad Autónoma Metropolitana Cuajimalpa (UAM-C), Pedro Antonio de los Santos 84, San-Miguel-Chapultepec, C.P. 11850 D.F, Mexico

Uribe-Carvajal S.:
 Univ Nacl Autonoma Mexico, IFC, Dept Mol Genet, Mexico City 04510, DF, Mexico

Ruiz-Granados Y.G.:
 Univ Nacl Autonoma Mexico, IFC, Dept Mol Genet, Mexico City 04510, DF, Mexico
ISSN: 10530509
Editorial
SPRINGER/PLENUM PUBLISHERS, 233 SPRING ST, NEW YORK, NY 10013 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 24 Número: 6
Páginas: 1849-1859
WOS Id: 000345643200031
ID de PubMed: 25345860

MÉTRICAS