Stimulation of F1-ATPase activity by sodium dodecyl sulfate

Mohammad Delawar Hossain, Shou Furuike, Yasuhiro Onoue, Kengo Adachi, Masasuke Yoshida, Kazuhiko Kinosita

    Research output: Contribution to journalArticle

    2 Citations (Scopus)

    Abstract

    F1-ATPase is a rotary molecular motor in which the γ subunit rotates inside the cylinder made of α3Β3 subunits. We have studied the effects of sodium dodecyl sulfate (SDS) on the rotational and ATP hydrolysis activities of F1-ATPase. Bulk hydrolysis activity at various SDS concentrations was examined at 2mM ATP. Maximal stimulation was obtained at 0.003% (w/v) SDS, the initial (least inhibited) activity being about 1.4 times and the steady-state activity 3-4 times the values in the absence of SDS. Rotation rates observed with a 40-nm gold bead or a 0.29-μm bead duplex as well as the torque were unaffected by the presence of 0.003% SDS. The fraction of beads that rotated, in contrast, tended to increase in the presence of SDS. SDS seems to bring inactive F1 molecules into an active form but it does not alter or enhance the function of already active F1 molecules significantly.

    Original languageEnglish
    Pages (from-to)435-442
    Number of pages8
    JournalBiochimica et Biophysica Acta - Bioenergetics
    Volume1797
    Issue number4
    DOIs
    Publication statusPublished - 2010 Apr

    Keywords

    • ATP hydrolysis
    • ATP synthase
    • Detergent
    • Optical microscopy
    • Single molecule
    • Torque

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Cell Biology

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  • Cite this

    Hossain, M. D., Furuike, S., Onoue, Y., Adachi, K., Yoshida, M., & Kinosita, K. (2010). Stimulation of F1-ATPase activity by sodium dodecyl sulfate. Biochimica et Biophysica Acta - Bioenergetics, 1797(4), 435-442. https://doi.org/10.1016/j.bbabio.2009.12.018