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Photoaffmity cross‐linking of F 1 ATPase from the thermophilic bacterium PS 3 by 3'‐arylazido‐β‐alanyl‐8‐azido ATP
Author(s) -
Schäfer Hans-Jochen,
Rathgeber Gabriele,
Dose Klaus,
Masafumi Y.,
Kagawa Y.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80724-9
Subject(s) - thermophile , nucleotide , atp hydrolysis , atpase , chemistry , biochemistry , adenosine triphosphate , bacteria , bifunctional , ultraviolet light , enzyme , biophysics , stereochemistry , biology , photochemistry , genetics , gene , catalysis
To study the localization of the nucleotide binding sites of coupling factor 1 (TF 1 ) from the thermophilic bacterium PS3 we used the bifunctional (cross‐linking) 3'‐arylazido‐β‐alanyl‐8‐azido ATP (DiN 3 ATP) for photoaffinity labeling. DiN 3 ATP is hydrolyzed by TF 1 in the absence of ultraviolet light. Irradiation (UV light) of TF 1 in the presence of DiN 3 ATP results in a nucleotide‐specific reduction of ATPase activity and in a nucleotide‐specific formation of different cross‐linked proteins (dimers, trimers, oligomers) formed by the major subunits α and/or β. The results suggest that nucleotide binding sites (one, two, possibly all) are located at the interfaces between these subunits.