Descripción: The subfilter-scale (SFS) physics of regularization models are investigated to understand the regularizations' performance as SFS models. Suppression of spectrally local SFS interactions and conservation of small-scale circulation in the Lagrangian-averaged Navier-Stokes α-model (LANS-α) is found to lead to the formation of rigid bodies. These contaminate the superfilter-scale energy spectrum with a scaling that approaches k +1 as the SFS spectra is resolved. The Clark-α and Leray-α models, truncations of LANS-α, do not conserve small-scale circulation and do not develop rigid bodies. LANS-α, however, is closest to Navier-Stokes in intermittency properties. All three models are found to be stable at high Reynolds number. Differences between L 2 and H 1 norm models are clarified. For magnetohydrodynamics (MHD), the presence of the Lorentz force as a source (or sink) for circulation and as a facilitator of both spectrally nonlocal large to small scale interactions as well as local SFS interactions prevents the formation of rigid bodies in Lagrangian-averaged MHD (LAMHD-α). LAMHD-α performs well as a predictor of superfilter-scale energy spectra and of intermittent current sheets at high Reynolds numbers. It may prove generally applicable as a MHD-LES. © 2010 Springer Science+Business Media, LLC.

Descripción: Stress granules (SGs) and P-bodies (PBs) are related cytoplasmic structures harboring silenced mRNAs. SGs assemble transiently upon cellular stress, whereas PBs are constitutive and are further induced by stress. Both foci are highly dynamic, with messenger ribonucleoproteins (mRNPs) and proteins rapidly shuttling in and out. Here, we show that impairment of retrograde transport by knockdown of mammalian dynein heavy chain 1 (DHC1) or bicaudal D1 (BicD1) inhibits SG formation and PB growth upon stress, without affecting proteinsynthesis blockage. Conversely, impairment of anterograde transport by knockdown of kinesin-1 heavy chain (KIF5B) or kinesin light chain 1 (KLC1) delayed SG dissolution. Strikingly, SG dissolution is not required to restore translation. Simultaneous knockdown of dynein and kinesin reverted the effect of single knockdowns on both SGs and PBs, suggesting that a balance between opposing movements driven by these molecular motors governs foci formation and dissolution. Finally, we found that regulation of SG dynamics by dynein and kinesin is conserved in Drosophila.

Descripción: We generated a map of wetlands in Argentina from the digital edition of the National Soil Inventory made by the National Institute of Agricultural Technology (Instituto Nacional de Tecnología Agropecuaria, INTA). Potencial wetland areas were extracted from the map after an exhaustive analysis of the database and reassignment of the soil classes, by taking into account 1) soil taxonomic classes; 2) constraining factors (waterlogging, flooding, drainage impairment); and 3) cartographic categories, including lakes, lagoons, marshes and salt lakes. Estimated wetland area is about 600,000 km2, representing 21.5% of the national territory; it increases to 23% when considering salt lakes and deepwater bodies, but their surface is underestimated in the INTA database. Finally, we analyzed the distribution and abundance of wetland areas from different eco-regions of Argentina, and compared our results with current global wetland databases.

Descripción: The p53 tumor suppressor protein is an important regulator of cell proliferation and apoptosis. p53 can be found in the nucleus and in the cytosol, and the subcellular location is key to control p53 function. In this work, we found that a widely used monoclonal antibody against p53, termed Pab 1801 (Pan antibody 1801) yields a remarkable punctate signal in the cytoplasm of several cell lines of human origin. Surprisingly, these puncta were also observed in two independent p53-null cell lines. Moreover, the foci stained with the Pab 1801 were present in rat cells, although Pab 1801 recognizes an epitope that is not conserved in rodent p53. In contrast, the Pab 1801 nuclear staining corresponded to genuine p53, as it was upregulated by p53-stimulating drugs and absent in p53-null cells. We identified the Pab 1801 cytoplasmic puncta as P Bodies (PBs), which are involved in mRNA regulation. We found that, in several cell lines, including U2OS, WI38, SK-N-SH and HCT116, the Pab 1801 puncta strictly colocalize with PBs identified with specific antibodies against the PB components Hedls, Dcp1a, Xrn1 or Rck/p54. PBs are highly dynamic and accordingly, the Pab 1801 puncta vanished when PBs dissolved upon treatment with cycloheximide, a drug that causes polysome stabilization and PB disruption. In addition, the knockdown of specific PB components that affect PB integrity simultaneously caused PB dissolution and the disappearance of the Pab 1801 puncta. Our results reveal a strong cross-reactivity of the Pab 1801 with unknown PB component(s). This was observed upon distinct immunostaining protocols, thus meaning a major limitation on the use of this antibody for p53 imaging in the cytoplasm of most cell types of human or rodent origin. © 2012 Thomas et al.

Descripción: Stress granules are cytoplasmic mRNA-silencing foci that form transiently during the stress response. Stress granules harbor abortive translation initiation complexes and are in dynamic equilibrium with translating polysomes. Mammalian Staufen 1 (Stau1) is a ubiquitous double-stranded RNA-binding protein associated with polysomes. Here, we show that Stau1 is recruited to stress granules upon induction of endoplasmic reticulum or oxidative stress as well in stress granules induced by translation initiation blockers. We found that stress granules lacking Stau1 formed in cells depleted of this molecule, indicating that Stau1 is not an essential component of stress granules. Moreover, Stau1 knockdown facilitated stress granule formation upon stress induction. Conversely, transient transfection of Stau1 impaired stress granule formation upon stress or pharmacological initiation arrest. The inhibitory capacity of Stau1 mapped to the amino-terminal half of the molecule, a region known to bind to polysomes. We found that the fraction of polysomes remaining upon stress induction was enriched in Stau1, and that Stau1 overexpression stabilized polysomes against stress. We propose that Stau1 is involved in recovery from stress by stabilizing polysomes, thus helping stress granule dissolution.