6533b7d8fe1ef96bd126a520
RESEARCH PRODUCT
Photoaffinity cross-linking of F1ATPase from the thermophilic bacterium PS3 by 3′-arylazido-β-alanyl-2-azido ATP
Hans-jochen SchäferGabriele RathgeberKlaus DoseYasuo Kagawasubject
chemistry.chemical_classificationMolecular massbiologyStereochemistryProtein subunitNucleotide conformationBiophysicsCell Biologybiology.organism_classificationBiochemistrychemistry.chemical_compoundEnzymechemistryStructural BiologyGeneticsPhotoaffinity crosslinkingATPase F1-NucleotideNucleotide-binding siteBinding siteBifunctionalInterfacial localizationMolecular BiologyThermophilic bacterium PS3Bacteriadescription
AbstractThe photoactivatable bifunctional 3′-arylazido-β-alanyl-2-azido ATP (2,3′-DiN3ATP) has been applied to study the localization of the nucleotide-binding sites of coupling factor 1 (F1ATPase, TF1) from the thermophilic bacterium PS3 by photoaffinity cross-linking. UV irradiation of TF1 in the presence of 2,3′-DiN3ATP results in the nucleotide-dependent formation of various higher molecular mass cross-links formed by two, three or even four α- and/or β-subunits. The differences observed upon photoaffinity cross-linking by the bifunctional 2-azido ATP or 8-azido ATP analog are discussed. They are probably due to the varied maximal distance between both azido groups, or to the different conformations (anti/syn) of these analogs. The results confirm our suggestion that several (possibly all) nucleotide-binding sites of F1ATPases are located at the interfaces between α- and β-subunits.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1989-08-14 | FEBS Letters |