Catalytic robustness and torque generation of the F1-ATPase

Noji, Hiroyuki; Ueno, Hiroshi; McMillan, Duncan G. G.

doi:10.1007/s12551-017-0262-x

Cited by 51 publications

(48 citation statements)

References 120 publications

(198 reference statements)

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“…Generally, respirable bacteria generate a proton gradient across the cell membrane in the respiratory process. The proton gradient causes proton motive force which drives F-type ATP synthase and bacterial flagella (55, 56). However, Mycoplasmas have no genes for electron transport and synthesize ATP molecules by glycolysis (57).…”

Section: Discussionmentioning

confidence: 99%

Behaviors and Energy Source ofMycoplasma gallisepticumGliding

Mizutani

Miyata

2019

Preprint

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Mycoplasma gallisepticum, an avian-pathogenic bacterium, glides on host tissue surfaces by using a common motility system with Mycoplasma pneumoniae. In the present study, we observed and analyzed the gliding behaviors of M. gallisepticum in detail by using optical microscopes. M. gallisepticum glided at a speed of 0.27 ± 0.09 µm/s with directional changes relative to the cell axis of 0.6 ± 44.6 degrees/5 s without the rolling of the cell body. To examine the effects of viscosity on gliding, we analyzed the gliding behaviors under viscous environments. The gliding speed was constant in various concentrations of methylcellulose but was affected by Ficoll. To investigate the relationship between binding and gliding, we analyzed the inhibitory effects of sialyllactose on binding and gliding. The binding and gliding speed sigmoidally decreased with sialyllactose concentration, indicating the cooperative binding of the cell. To determine the direct energy source of gliding, we used a membrane-permeabilized ghost model. We permeabilized M. gallisepticum cells with Triton X-100 or Triton X-100 containing ATP and analyzed the gliding of permeabilized cells. The cells permeabilized with Triton X-100 did not show gliding; in contrast, the cells permeabilized with Triton X-100 containing ATP showed gliding at a speed of 0.014 ± 0.007 μm/s. These results indicate that the direct energy source for the gliding motility of M. gallisepticum is ATP.IMPORTANCEMycoplasmas, the smallest bacteria, are parasitic and occasionally commensal. Mycoplasma gallisepticum is related to human pathogenic Mycoplasmas—Mycoplasma pneumoniae and Mycoplasma genitalium—which causes so-called ‘walking pneumonia’ and non-gonococcal urethritis, respectively. These Mycoplasmas trap sialylated oligosaccharides, which are common targets among influenza viruses, on host trachea or urinary tract surfaces and glide to enlarge the infected areas. Interestingly, this gliding motility is not related to other bacterial motilities or eukaryotic motilities. Here, we quantitatively analyze cell behaviors in gliding and clarify the direct energy source. The results provide clues for elucidating this unique motility mechanism.

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Section: Discussionmentioning

confidence: 99%

Behaviors and Energy Source ofMycoplasma gallisepticumGliding

Mizutani

Miyata

2019

Preprint

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“…When the electrochemical proton gradient is sufficient to impose a large Fo torque, the enzyme catalyses the synthesis of ATP from ADP and Pi. When the phosphate potential predominates, F 1 reverses the rotation of F O to build up a membrane potential (Noji et al, ). The OSCP (or δ) subunit located on top of F1 ensures the structural coupling between F O and F 1 .…”

Section: The Fof1 Atp Synthasementioning

confidence: 99%

“…Bacterial F O has the simplest subunit composition with (i) the ring of 10–15 c subunits, (ii) the membrane‐embedded subcomplex ab2 and (iii) the peripheral stalk comprising the extrinsic part of the b subunits and the F 1 subunit δ (Noji et al, ). In the mitochondrial enzyme, F O mediates the formation of V‐shaped F‐ATP synthase dimers (Hahn et al, ; Guo et al, ), which are not found in bacteria, and has a far more complex structure.…”

Section: The Fof1 Atp Synthasementioning

confidence: 99%

OSCP subunit of mitochondrial ATP synthase: role in regulation of enzyme function and of its transition to a pore

Giorgio¹,

Fogolari

Lippe

et al. 2018

British J Pharmacology

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The permeability transition pore (PTP) is a latent, high‐conductance channel of the inner mitochondrial membrane. When activated, it plays a key role in cell death and therefore in several diseases. The investigation of the PTP took an unexpected turn after the discovery that cyclophilin D (the target of the PTP inhibitory effect of cyclosporin A) binds to FOF1 (F)‐ATP synthase, thus inhibiting its catalytic activity by about 30%. This observation was followed by the demonstration that binding occurs at a particular subunit of the enzyme, the oligomycin sensitivity conferral protein (OSCP), and that F‐ATP synthase can form Ca2+‐activated, high‐conductance channels with features matching those of the PTP, suggesting that the latter originates from a conformational change in F‐ATP synthase. This review is specifically focused on the OSCP subunit of F‐ATP synthase, whose unique features make it a potential pharmacological target both for modulation of F‐ATP synthase and its transition to a pore. Linked Articles This article is part of a themed section on Mitochondrial Pharmacology: Featured Mechanisms and Approaches for Therapy Translation. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.22/issuetoc

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“…[20][21][22] Flagellum rotates its filament with proton-motive force (PMF) derived from the concentration gradient of protons across the inner membrane. 23) The γ subunit of F 0 F 1 -ATP synthase also rotates depending on PMF generated by mitochondrial electron transport system, and the rotation promotes ATP synthesis on α/β subunits. 24,25) Since T3SS is known to require PMF for effector secretion, 26) we hypothesized that effector proteins are exported by the T3SS needle similarly to PMF-dependent needle rotation.…”

Section: Similarities Of T3ss With Bacterial Flagellum and Atp Synthasementioning

confidence: 99%

Biophysical Mechanism of Protein Export by Bacterial Type III Secretion System

Ohgita

Saito

2019

CHEMICAL & PHARMACEUTICAL BULLETIN

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Type III secretion system (T3SS) is a protein injection nano-machine consisting of syringe and needlelike structure spanning bacterial inner and outer membranes. Bacteria insert the tip of T3SS needle to host cell membranes, and deliver effector proteins directly into host cells via T3SS to prime the host cell environment for infection. Thus inhibition of T3SS would be a potent strategy for suppressing bacterial infection. We previously demonstrated that T3SS needle rotates by proton-motive force (PMF) with the same mechanism as two evolutionally related rotary protein motors, flagellum and ATP synthase (FASEB J., 27, 2013, Ohgita et al.). Inhibition of needle rotation resulted in suppression of effector secretion, indicating the requirement of needle rotation for effector export. Simulation analysis of protein export by the T3SS needle suggests the importance of a hydrophobic helical groove formed by the conserved aromatic residue in the needle components. Based on these results, we have proposed a novel model of protein export by the T3SS needle, in which effector proteins are exported by PMF-dependent needle rotation oppositely to the hydrophobic helical groove in the needle. Quantitative examinations of the correlation between the speeds of T3SS rotation and the amount of effector export support this model. In this review, we summarize our current understanding of T3SS, and discuss our novel model of the protein export mechanism of T3SS based on the needle rotation.

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Catalytic robustness and torque generation of the F1-ATPase

Cited by 51 publications

References 120 publications

Behaviors and Energy Source ofMycoplasma gallisepticumGliding

Behaviors and Energy Source ofMycoplasma gallisepticumGliding

OSCP subunit of mitochondrial ATP synthase: role in regulation of enzyme function and of its transition to a pore

Biophysical Mechanism of Protein Export by Bacterial Type III Secretion System

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