The TF1-ATPase and ATPase activities of assembled α3β3γ, α3β3γδ, and α3β3γε complexes are stimulated by low and inhibited by high ... View Full Text


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Article Info

DATE

1993-12

AUTHORS

Seung R. Paik, Ken Yokoyama, Masasuke Yoshida, Toshiko Ohta, Yasuo Kagawa, William S. Allison

ABSTRACT

The ATPase activity of the F1-ATPase from the thermophilic bacterium PS3 is stimulated at concentrations of rhodamine 6G up to about 10 µM where 70% stimulation is observed at 36°C. Half maximal stimulation is observed at about 3 µM dye. At rhodamine 6G concentrations greater than 10 µM, ATPase activity declines with 50% inhibition observed at about 75 µM dye. The ATPase activities of the α3β3γ and α3β3γδ complexes assembled from isolated subunits of TF1 expressed inE. coli deleted of theunc operon respond to increasing concentrations of rhodamine 6G nearly identically to the response of TF1. In contrast, the ATPase activities of the α3β3 and α3β3δ complexes are only inhibited by rhodamine 6G with 50% inhibition observed, respectively, at 35 and 75 µM dye at 36°C. The ATPase activity of TF1 is stimulated up to 4-fold by the neutral detergent, LDAO. In the presence of stimulating concentrations of LDAO, the ATPase activity of TF1 is no longer stimulated by rhodamine 6G, but rather, it is inhibited with 50% inhibition observed at about 30 µM dye at 30°C. One interpretation of these results is that binding of rhodamine 6G to a high-affinity site on TF1 stimulates ATPase activity and unmasks a low-affinity, inhibitory site for the dye which is also exposed by LDAO. More... »

PAGES

679-684

References to SciGraph publications

  • 1992-10. The αβ complexes of ATP synthase: the α3β3 oligomer and α1β1 protomer in JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00770254

    DOI

    http://dx.doi.org/10.1007/bf00770254

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1082671663

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8144495


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