2,144 research outputs found

    Comparative Genomics of Campylobacter fetus from Reptiles and Mammals Reveals Divergent Evolution in Host-Associated Lineages

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    Acknowledgments The authors like to thank Brian Brooks and John Devenish (Canadian Food Inspection Agency) for providing strains and valuable suggestions.Peer reviewedPublisher PD

    Campylobacter fetus Subspecies Contain Conserved Type IV Secretion Systems on Multiple Genomic Islands and Plasmids

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    Acknowledgments We like to thank Dr. John Devenish and Dr. Brian Brooks (Canadian Food Inspection Agency) for providing strains. We thank Nathaniel Simon and Mary Chapman for the generation of Illumina MiSeq reads and we thank James Bono for the generation of PacBio RS reads. Funding: The authors have no support or funding to report.Peer reviewedPublisher PD

    Whole genome sequence analysis indicates recent diversification of mammal-associated Campylobacter fetus and implicates a genetic factor associated with H2S production

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    cknowledgements We like to thank Emma Yee (U.S. Department of Agriculture) for the generation of sequence data, we thank James Bono (U.S. Department of Agriculture) for the generation of PacBio RS reads and thank Dr. Brian Brooks and Dr. John Devenish (Canadian Food Inspection Agency) for providing C. fetus strains and for critical review of this manuscript. Funding Publication charges for this article have been funded by Utrecht University, the Netherlands.Peer reviewedPublisher PD

    Effect of turbulence on collisional growth of cloud droplets

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    We investigate the effect of turbulence on the collisional growth of um-sized droplets through high- resolution numerical simulations with well resolved Kolmogorov scales, assuming a collision and coalescence efficiency of unity. The droplet dynamics and collisions are approximated using a superparticle approach. In the absence of gravity, we show that the time evolution of the shape of the droplet-size distribution due to turbulence-induced collisions depends strongly on the turbulent energy-dissipation rate, but only weakly on the Reynolds number. This can be explained through the energy dissipation rate dependence of the mean collision rate described by the Saffman-Turner collision model. Consistent with the Saffman-Turner collision model and its extensions, the collision rate increases as the square root of the energy dissipation rate even when coalescence is invoked. The size distribution exhibits power law behavior with a slope of -3.7 between a maximum at approximately 10 um up to about 40 um. When gravity is invoked, turbulence is found to dominate the time evolution of an initially monodisperse droplet distribution at early times. At later times, however, gravity takes over and dominates the collisional growth. We find that the formation of large droplets is very sensitive to the turbulent energy dissipation rate. This is due to the fact that turbulence enhances the collisional growth between similar sized droplets at the early stage of raindrop formation. The mean collision rate grows exponentially, which is consistent with the theoretical prediction of the continuous collisional growth even when turbulence-generated collisions are invoked. This consistency only reflects the mean effect of turbulence on collisional growth

    Functional Analysis of Subunit e of the F\u3csub\u3e1\u3c/sub\u3eF\u3csub\u3eo\u3c/sub\u3e-ATP Synthase of the Yeast \u3cem\u3eSaccharomyces cerevisiae\u3c/em\u3e: Importance of the N-Terminal Membrane Anchor Region

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    Mitochondrial F1Fo-ATP synthase complexes do not exist as physically independent entities but rather form dimeric and possibly oligomeric complexes in the inner mitochondrial membrane. Stable dimerization of two F1Fo-monomeric complexes involves the physical association of two membrane-embedded Fo-sectors. Previously, formation of the ATP synthase dimeric-oligomeric network was demonstrated to play a critical role in modulating the morphology of the mitochondrial inner membrane. In Saccharomyces cerevisiae, subunit e (Su e) of the Fo-sector plays a central role in supporting ATP synthase dimerization. The Su e protein is anchored to the inner membrane via a hydrophobic region located at its N-terminal end. The hydrophilic C-terminal region of Su e resides in the intermembrane space and contains a conserved coiled-coil motif. In the present study, we focused on characterizing the importance of these regions for the function of Su e. We created a number of C-terminal-truncated derivatives of the Su e protein and expressed them in the Su e null yeast mutant. Mitochondria were isolated from the resulting transformant strains, and a number of functions of Su e were analyzed. Our results indicate that the N-terminal hydrophobic region plays important roles in the Su e-dependent processes of mitochondrial DNA maintenance, modulation of mitochondrial morphology, and stabilization of the dimer-specific Fo subunits, subunits g and k. Furthermore, we show that the C-terminal coiled-coil region of Su e functions to stabilize the dimeric form of detergent-solubilized ATP synthase complexes. Finally, we propose a model to explain how Su e supports the assembly of the ATP synthase dimers-oligomers in the mitochondrial membrane
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