NDLI: Redox Regulation of Rotation of the Cyanobacterial F1-ATPase Containing Thiol Regulation Switch*

Content Provider	PubMed Central
Author	Kim, Yusung Konno, Hiroki Sugano, Yasushi Hisabori, Toru
Abstract	F1-ATP synthase (F1-ATPase) is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis. Chloroplast F1-ATPase is subject to redox regulation, whereby ATP hydrolysis activity is regulated by formation and reduction of the disulfide bond located on the γ subunit. To understand the molecular mechanism of this redox regulation, we constructed a chimeric F1 complex (α3β3γredox) using cyanobacterial F1, which mimics the regulatory properties of the chloroplast F1-ATPase, allowing the study of its regulation at the single molecule level. The redox state of the γ subunit did not affect the ATP binding rate to the catalytic site(s) and the torque for rotation. However, the long pauses caused by ADP inhibition were frequently observed in the oxidized state. In addition, the duration of continuous rotation was relatively shorter in the oxidized α3β3γredox complex. These findings lead us to conclude that redox regulation of CF1-ATPase is achieved by controlling the probability of ADP inhibition via the γ subunit inserted region, a sequence feature observed in both cyanobacterial and chloroplast ATPase γ subunits, which is important for ADP inhibition (Sunamura, E., Konno, H., Imashimizu-Kobayashi, M., Sugano, Y., and Hisabori, T. (2010) Plant Cell Physiol. 51, 855–865).
Related Links	http://dx.doi.org/10.1074/jbc.m110.200584
Ending Page	9078
Page Count	8
Starting Page	9071
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	11
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-03-18
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Redox Regulation of Rotation of the Cyanobacterial F1-ATPase Containing Thiol Regulation Switch

A Conformational Change of the γ Subunit Indirectly Regulates the Activity of Cyanobacterial F1-ATPase

Characterization of the Relationship between ADP- and ϵ-induced Inhibition in Cyanobacterial F1-ATPase*

A Conformational Change of the γ Subunit Indirectly Regulates the Activity of Cyanobacterial F1-ATPase*

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Redox Regulation of Rotation of the Cyanobacterial F1-ATPase Containing Thiol Regulation Switch*

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