NDLI: Subunit Positioning and Stator Filament Stiffness in Regulation and Power Transmission in the V1 Motor of the Manduca sexta V-ATPase ☆

Content Provider	PubMed Central
Author	Muench, Stephen P. Scheres, Sjors H. W. Huss, Markus Phillips, Clair Olga, Vitavska Wieczorek, Helmut John, Trinick Harrison, Michael A.
Copyright Year	2013
Abstract	The vacuolar H+-ATPase (V-ATPase) is an ATP-driven proton pump essential to the function of eukaryotic cells. Its cytoplasmic V1 domain is an ATPase, normally coupled to membrane-bound proton pump Vo via a rotary mechanism. How these asymmetric motors are coupled remains poorly understood. Low energy status can trigger release of V1 from the membrane and curtail ATP hydrolysis. To investigate the molecular basis for these processes, we have carried out cryo-electron microscopy three-dimensional reconstruction of deactivated V1 from Manduca sexta. In the resulting model, three peripheral stalks that are parts of the mechanical stator of the V-ATPase are clearly resolved as unsupported filaments in the same conformations as in the holoenzyme. They are likely therefore to have inherent stiffness consistent with a role as flexible rods in buffering elastic power transmission between the domains of the V-ATPase. Inactivated V1 adopted a homogeneous resting state with one open active site adjacent to the stator filament normally linked to the H subunit. Although present at 1:1 stoichiometry with V1, both recombinant subunit C reconstituted with V1 and its endogenous subunit H were poorly resolved in three-dimensional reconstructions, suggesting structural heterogeneity in the region at the base of V1 that could indicate positional variability. If the position of H can vary, existing mechanistic models of deactivation in which it binds to and locks the axle of the V-ATPase rotary motor would need to be re-evaluated.
Related Links	http://dx.doi.org/10.1016/j.jmb.2013.09.018
Ending Page	300
Page Count	15
Starting Page	286
File Format	PDF
ISSN	10898638
e-ISSN	10898638
Journal	Journal of Molecular Biology
Issue Number	2
Volume Number	426
Language	English
Publisher	Elsevier
Publisher Date	2014-01-23
Access Restriction	Open
Rights Holder	Elsevier
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology Biophysics

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