Regular ArticleAmino Acid Substitutions in theaSubunit Affect the ϵ Subunit of F1F0ATP Synthase fromEscherichia coli☆
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Cited by (20)
The b subunits in the peripheral stalk of F<inf>1</inf>F<inf>0</inf> ATP synthase preferentially adopt an offset relationship
2009, Journal of Biological ChemistryIntrinsic uncoupling in the ATP synthase of Escherichia coli
2008, Biochimica et Biophysica Acta - BioenergeticsCitation Excerpt :The possibility of modulating the coupling efficiency might require the existence of a structural device acting somehow as a clutch. The ɛ subunit appears to us as a possible candidate for this role, since it has frequently been indicated as a key regulatory and structural feature in the coupling mechanism (see e.g. [13–18,54] and for reviews [55–58]). In particular, the drastic changes in the ɛ trypsinization pattern induced by Pi [48] are consistent with Pi triggering the interconversion between two conformations, and the occurrence of drastically different conformations in this subunit has been confirmed by structural [59,60] and mutational studies [38,39].
The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli
2003, Archives of Biochemistry and BiophysicsCitation Excerpt :Assays were conducted in the presence of LDAO, as an indicator of the level of F1 ATPase present in the membrane preparations. Some mutations in ATP synthase subunits are known to cause variable inhibition of ATP hydrolysis due to the ε subunit [48,49]. Since LDAO relieves inhibition by ε [50], its inclusion in the assay medium will result in a rate of ATP hydrolysis that correlates with the amount of F1 present.
Genetic fusions of globular proteins to the ε subunit of the Eescherichia coli ATP synthase. Implications for in vivo rotational catalysis and ε subunit function
2002, Journal of Biological ChemistryCitation Excerpt :In addition, Mendel-Hartvig and Capaldi (54) found that the nucleotide-dependent conformational change of ε in ATP synthase was blocked by treatment with DCCD, again implying that partial rotation of the N-terminal domain of ε, and the attached ring of c subunits, is an essential part of the change. Recently, Gardner and Cain (59) reported that nucleotide-dependent conformational changes in ε are impaired by mutations such as G218D in the a subunit. Furthermore, the residual ATPase activity of the aR210I mutant was uncoupled but DCCD-sensitive, like the larger ε fusions.
The a subunit ala-217 → arg substitution affects catalytic activity of F<inf>1</inf> F<inf>0</inf> ATP synthase
2000, Archives of Biochemistry and Biophysics
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Funding for this investigation was provided by the United States Public Health Service Grant R01-GM43495.
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To whom correspondence should be addressed at Department of Biochemistry and Molecular Biology, Box 100245, University of Florida, Gainesville, FL 32610. Fax: (352) 392-2953. E-mail:[email protected].