Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals

Jiko, Chimari; Davies, Karen M.; Shinzawa‐Itoh, Kyoko; Tani, Kazuhide; Maeda, Shuichi; Mills, Deryck J.; Tsukihara, Tomitake; Fujiyoshi, Yoshinori; Kühlbrandt, Werner; Gerle, Christoph

doi:10.7554/elife.06119

Cited by 75 publications

(64 citation statements)

References 44 publications

(88 reference statements)

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“…Furthermore, a E and b DP shift away from the central g subunit and interact with the peripheral stalk, which is not present in the F 1 crystal structure. Recently a contact between peripheral stalk and the lower domain of a E was also observed for the membrane-embedded bovine holoenzyme (Jiko et al, 2015). In line with the results of a crosslinking study on the bacterial F o F 1 holoenzyme in synthesis mode (Masaike et al, 2006), this IMPs are solubilized in lauryl maltose-neopentyl glycol (LMNG) either by direct extraction or after exchange from another detergent.…”

Section: D Cryo-em Analysis Of Mammalian F O F 1 Atp Synthase Using mentioning

confidence: 60%

GraDeR: Membrane Protein Complex Preparation for Single-Particle Cryo-EM

et al. 2015

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We developed a method, named GraDeR, which substantially improves the preparation of membrane protein complexes for structure determination by single-particle cryo-electron microscopy (cryo-EM). In GraDeR, glycerol gradient centrifugation is used for the mild removal of free detergent monomers and micelles from lauryl maltose-neopentyl glycol detergent stabilized membrane complexes, resulting in monodisperse and stable complexes to which standard processes for water-soluble complexes can be applied. We demonstrate the applicability of the method on three different membrane complexes, including the mammalian FoF1 ATP synthase. For this highly dynamic and fragile rotary motor, we show that GraDeR allows visualizing the asymmetry of the F1 domain, which matches the ground state structure of the isolated domain. Therefore, the present cryo-EM structure of FoF1 ATP synthase provides direct structural evidence for Boyer's binding change mechanism in the context of the intact enzyme.

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Section: D Cryo-em Analysis Of Mammalian F O F 1 Atp Synthase Using mentioning

confidence: 60%

GraDeR: Membrane Protein Complex Preparation for Single-Particle Cryo-EM

et al. 2015

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“…The differences in the length of the sides allowed us to unambiguously assign the α and β subunits and hence the catalytic and noncatalytic αβ interfaces (4). As in the yeast and bovine complex (10,13,17,20,30) the peripheral stalk extends along a noncatalytic interface. The bovine peripheral stalk did not fit the P. tetraurelia subtomogram average well, as it curves in the opposite direction (Fig.…”

Section: Significancementioning

confidence: 99%

Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria

Muhleip

Joos

Wigge

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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F 1 F o -ATP synthases are universal energy-converting membrane protein complexes that synthesize ATP from ADP and inorganic phosphate. In mitochondria of yeast and mammals, the ATP synthase forms V-shaped dimers, which assemble into rows along the highly curved ridges of lamellar cristae. Using electron cryotomography and subtomogram averaging, we have determined the in situ structure and organization of the mitochondrial ATP synthase dimer of the ciliate Paramecium tetraurelia. The ATP synthase forms U-shaped dimers with parallel monomers. Each complex has a prominent intracrista domain, which links the c-ring of one monomer to the peripheral stalk of the other. Close interaction of intracrista domains in adjacent dimers results in the formation of helical ATP synthase dimer arrays, which differ from the loose dimer rows in all other organisms observed so far. The parameters of the helical arrays match those of the cristae tubes, suggesting the unique features of the P. tetraurelia ATP synthase are directly responsible for generating the helical tubular cristae. We conclude that despite major structural differences between ATP synthase dimers of ciliates and other eukaryotes, the formation of ATP synthase dimer rows is a universal feature of mitochondria and a fundamental determinant of cristae morphology.cryoelectron microscopy | subtomogram averaging | Paramecium | macromolecular organization | serial block face imaging F 1 F o -ATP synthases are ubiquitous, highly conserved energyconverting membrane protein complexes. ATP synthases produce ATP from ADP and inorganic phosphate (P i ) by rotary catalysis (1, 2) using the energy stored in a transmembrane electrochemical gradient. The ∼600-kDa monomer of the mitochondrial ATP synthase is composed of a soluble F 1 subcomplex and a membranebound F o subcomplex (3). The main components of the F 1 subcomplex are the (αβ) 3 hexamer and the central stalk (4). The F o subcomplex includes a rotor ring of 8-15 hydrophobic c subunits (5), the peripheral stalk, and several small hydrophobic stator subunits. Protons flowing through the membrane part of the F o subcomplex drive the rotation of the c-ring (6-9). The central stalk transmits the torque generated by c-ring rotation to the catalytic head of the F 1 subcomplex, where it induces conformational changes of the α and β subunits that result in phosphate bond formation and the generation of ATP. The catalytic (αβ) 3 hexamer is held stationary relative to the membrane region by the peripheral stalk (10, 11). Several high-resolution structures of the F 1 /rotor ring complexes have been solved by X-ray crystallography (12-16), and the structure of the complete assembly has been determined by cryoelectron microscopy (cryo-EM) (10,(17)(18)(19)(20).In mitochondria, the ATP synthase forms dimers in the inner membrane. In fungi, plants, and metazoans, the dimers are V-shaped and associate into rows along the highly curved ridges of lamellar cristae (19)(20)(21)(22). F o subcomplexes of the two monomers in the dimer interact in...

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“…The best characterized example of membrane curvature generation by an integral membrane protein is the F o F 1 ATP synthase, which resides in the highly curved membranes of mitochondrial cristae. Recent cryo-ET studies demonstrate that the shape of enzyme monomers imparts an intrinsic kink in the surrounding bilayer (Baker et al, 2012), and dimerization conjoins kinks to generate substantial membrane curvature (Jiko et al, 2015). …”

Section: Molecular Basis For Os Architecturementioning

confidence: 99%

Molecular basis for photoreceptor outer segment architecture

Goldberg

Moritz

Williams

2016

Progress in Retinal and Eye Research

158

160

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To serve vision, vertebrate rod and cone photoreceptors must detect photons, convert the light stimuli into cellular signals, and then convey the encoded information to downstream neurons. Rods and cones are sensory neurons that each rely on specialized ciliary organelles to detect light. These organelles, called outer segments, possess elaborate architectures that include many hundreds of light-sensitive membranous disks arrayed one atop another in precise register. These stacked disks capture light and initiate the chain of molecular and cellular events that underlie normal vision. Outer segment organization is challenged by an inherently dynamic nature; these organelles are subject to a renewal process that replaces a significant fraction of their disks (up to ~10%) on a daily basis. In addition, a broad range of environmental and genetic insults can disrupt outer segment morphology to impair photoreceptor function and viability. In this chapter, we survey the major progress that has been made for understanding the molecular basis of outer segment architecture. We also discuss key aspects of organelle lipid and protein composition, and highlight distributions, interactions, and potential structural functions of key OS-resident molecules, including: kinesin-2, actin, RP1, prominin-1, protocadherin 21, peripherin-2/rds, rom-1, glutamic acid-rich proteins, and rhodopsin. Finally, we identify key knowledge gaps and challenges that remain for understanding how normal outer segment architecture is established and maintained.

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Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals

Cited by 75 publications

References 44 publications

GraDeR: Membrane Protein Complex Preparation for Single-Particle Cryo-EM

GraDeR: Membrane Protein Complex Preparation for Single-Particle Cryo-EM

Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria

Molecular basis for photoreceptor outer segment architecture

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