Escherichia coli F1Fo-ATP Synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits

Chathurada S. Gajadeera; Joachim Weber

doi:10.1074/jbc.M113.503722

Escherichia coli F₁F_o-ATP Synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits

Chathurada S. Gajadeera, Joachim Weber

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

Background: The essential "stator stalk" connects the nonrotating portions of F₁F_o-ATP synthase. Results: A b/δ fusion protein is functional and allows analyzing the role of the individual b subunits. Conclusion: One of the b subunits is required for binding to F ₁, the other for binding to F_o. Significance: Understanding the function of the stator stalk is important for understanding the mechanism of ATP synthase.

Original language	English
Pages (from-to)	26441-26447
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	288
Issue number	37
DOIs	https://doi.org/10.1074/jbc.M113.503722
State	Published - Sep 13 2013

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AB - Background: The essential "stator stalk" connects the nonrotating portions of F1Fo-ATP synthase. Results: A b/δ fusion protein is functional and allows analyzing the role of the individual b subunits. Conclusion: One of the b subunits is required for binding to F 1, the other for binding to Fo. Significance: Understanding the function of the stator stalk is important for understanding the mechanism of ATP synthase.

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Escherichia coli F₁F_o-ATP Synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits

Abstract

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