5 research outputs found

    A Burkholderia pseudomallei toxin inhibits helicase activity of translation factor eIF4A

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    The structure of BPSL1549, a protein of unknown function from Burkholderia pseudomallei, reveals a similarity to Escherichia coli cytotoxic necrotizing factor 1. We found that BPSL1549 acted as a potent cytotoxin against eukaryotic cells and was lethal when administered to mice. Expression levels of bpsl1549 correlate with conditions expected to promote or suppress pathogenicity. BPSL1549 promotes deamidation of glutamine-339 of the translation initiation factor eIF4A, abolishing its helicase activity and inhibiting translation. We propose to name BPSL1549 Burkholderia lethal factor 1

    Profile measurements of blowing snow at Halley, Antarctica

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    Measurements of blowing snow particle concentration from the second Stable Antarctic Boundary Layer Experiment (STABLE 2) are presented. The measurements, made at Halley Station (75.6 degreesS, 26.7 degreesW) throughout the 1991 austral winter, are supplemented with profile measurements of wind speed, air temperature, and humidity. Threshold wind speeds for blowing snow are shown to be distinctly different for various episodes, often depending strongly on the the availability of loose snow. Blowing snow is measured to occur at Halley between 27 and 37% of the time during winter. Total winter (June, July, August) blowing snow sublimation at Halley is calculated to be around 4.7 mm water equivalent, 3.7% of total accumulation over the same period. Total winter blowing snow mass transport is calculated to be around 5.5 x 10(5) kg per metre width. Measured humidity profiles at Halley show that during winter blowing snow conditions, a layer of near-saturated air forms, causing total sublimation to be less than that for seasonal or limited fetch snow covers. The extent of sublimation is shown to be strongly dependent on wind speed, temperature and fetch

    Wind-borne redistribution of snow across an Antarctic ice rise

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    Redistribution of snow by the wind can drive spatial and temporal variations in snow accumulation that may affect the reconstruction of paleoclimate records from ice cores. In this paper we investigate how spatial variations in snow accumulation along a 13 km transect across Lyddan Ice Rise, Antarctica, are related to wind-borne snow redistribution. Lyddan Ice Rise is an approximately two-dimensional ridge which rises about 130 m above the surrounding ice shelves. Local slopes on its flanks never exceed 0.04. Despite this very smooth profile, there is a pronounced gradient in snow accumulation across the feature. Accumulation is highest on the ice shelf to the east ( climatologically upwind) of the ice rise and decreases moving westward, with the lowest accumulation seen to the west ( climatologically downwind) of the ice rise crest. Superimposed on this broad-scale gradient are large ( 20-30%), localized variations in accumulation on a scale of around 1 km that appear to be associated with local variations in surface slope of less than 0.01. The broad-scale accumulation gradient is consistent with estimates of wind-borne redistribution of snow made using wind speed observations from three automatic weather stations. The small-scale variability in accumulation is reproduced quite well using a snow transport model driven by surface winds obtained from an airflow model, providing that both the wind shear and static stability of the upwind flow are taken into account. We conclude that great care needs to be exercised in selecting ice core sites in order to avoid the possibility of blowing snow transport confounding climate reconstructions

    Molecular basis of specificity and deamidation of eIF4A by Burkholderia lethal factor 1

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    Burkholderia pseudomallei lethal factor 1 (BLF1) exhibits site-specific glutamine deamidase activity against the eukaryotic RNA helicase, eIF4A, thereby blocking mammalian protein synthesis. The structure of a complex between BLF1 C94S and human eIF4A shows that the toxin binds in the cleft between the two RecA-like eIF4A domains forming interactions with residues from both and with the scissile amide of the target glutamine, Gln339, adjacent to the toxin active site. The RecA-like domains adopt a radically twisted orientation compared to other eIF4A structures and the nature and position of conserved residues suggests this may represent a conformation associated with RNA binding. Comparison of the catalytic site of BLF1 with other deamidases and cysteine proteases reveals that they fall into two classes, related by pseudosymmetry, that present either the re or si faces of the target amide/peptide to the nucleophilic sulfur, highlighting constraints in the convergent evolution of their Cys-His active sites
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