Single-molecule study on the temperature-sensitive reaction of F1-ATPase with a hybrid F1 carrying a single beta(E190D).

ABSTRACT: F(1)-ATPase is a rotary molecular motor in which the gamma-subunit rotates against the alpha(3)beta(3) cylinder. The unitary gamma-rotation is a 120 degrees step comprising 80 and 40 degrees substeps, each of these initiated by ATP binding and ADP release and by ATP hydrolysis and inorganic phosphate release, respectively. In our previous study on gamma-rotation at low temperatures, a highly temperature-sensitive (TS) reaction step of F(1)-ATPase from thermophilic Bacillus PS3 was found below 9 degrees C as an intervening pause before the 80 degrees substep at the same angle for ATP binding and ADP release. However, it remains unclear as to which reaction step the TS reaction corresponds. In this study, we found that the mutant F(1)(beta E190D) from thermophilic Bacillus PS3 showed a clear

SUBMITTER: Enoki S 

PROVIDER: S-EPMC2755722 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature