Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/83414
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dc.contributor.authorHotra, Adamen
dc.contributor.authorSuter, Manuelen
dc.contributor.authorBiuković, Goranen
dc.contributor.authorPriya, Ragunathanen
dc.contributor.authorKundu, Subhashrien
dc.contributor.authorDick, Thomasen
dc.contributor.authorGrüber, Gerharden
dc.date.accessioned2016-08-29T08:47:45Zen
dc.date.accessioned2019-12-06T15:21:59Z-
dc.date.available2016-08-29T08:47:45Zen
dc.date.available2019-12-06T15:21:59Z-
dc.date.issued2016en
dc.identifier.citationHotra, A., Suter, M., Biuković, G., Priya, R., Kundu, S., Dick, T., et al. (2016). Deletion of a unique loop in the mycobacterial F-ATP synthase γ subunit sheds light on its inhibitory role in ATP hydrolysis-driven H+ pumping. FEBS Journal, 283(10), 1947-1961.en
dc.identifier.issn1742-464Xen
dc.identifier.urihttps://hdl.handle.net/10356/83414-
dc.description.abstractThe F1FO-ATP synthase is one of the enzymes that is essential to meet the energy requirement of both the proliferating aerobic and hypoxic dormant stages of the life cycle of mycobacteria. Most F-ATP synthases consume ATP in the α3:β3 headpiece to drive the γ subunit, which couples ATP cleavage with proton pumping in the c ring of FO via the bottom of the γ subunit. ATPase-driven H+ pumping is latent in mycobacteria. The presence of a unique 14 amino acid residue loop of the mycobacterial γ subunit has been described and aligned in close vicinity to the c-ring loop Priya R et al. (2013) J Bioenerg Biomembr 45, 121-129 Here, we used inverted membrane vesicles (IMVs) of fast-growing Mycobacterium smegmatis and a variety of covalent and non-covalent inhibitors to characterize the ATP hydrolysis activity of the F-ATP synthase inside IMVs. These vesicles formed a platform to investigate the function of the unique mycobaterial γ loop by deleting the respective loop-encoding sequence (γ166–179) in the genome of M. smegmatis. ATP hydrolysis-driven H+ pumping was observed in IMVs containing the Δγ166–179 mutant protein but not for IMVs containing the wild-type F-ATP synthase. In addition, when compared to the wild-type enzyme, IMVs containing the Δγ166–179 mutant protein showed increased ATP cleavage and lower levels of ATP synthesis, demonstrating that the loop affects ATPase activity, ATPase-driven H+ pumping and ATP synthesis. These results further indicate that the loop may affect coupling of ATP hydrolysis and synthesis in a different mode.en
dc.description.sponsorshipNMRC (Natl Medical Research Council, S’pore)en
dc.description.sponsorshipMOH (Min. of Health, S’pore)en
dc.format.extent64 p.en
dc.language.isoenen
dc.relation.ispartofseriesFEBS Journalen
dc.rights© 2016 Federation of European Biochemical Societies. This is the author created version of a work that has been peer reviewed and accepted for publication in FEBS Journal, published by John Wiley & Sons, Inc. on behalf of Federation of European Biochemical Societies. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document.  The published version is available at: [http://dx.doi.org/10.1111/febs.13715].en
dc.subjectBioenergeticsen
dc.subjectFATP synthaseen
dc.titleDeletion of a unique loop in the mycobacterial F-ATP synthase γ subunit sheds light on its inhibitory role in ATP hydrolysis-driven H+ pumpingen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.contributor.schoolSchool of Physical and Mathematical Sciencesen
dc.contributor.schoolInterdisciplinary Graduate School (IGS)en
dc.identifier.doi10.1111/febs.13715en
dc.description.versionAccepted versionen
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