Molecular Modeling analysis of Wat1 and its interaction with Prp2.

<p><b>A.</b> 3D model of <i>S. pombe</i> Wat1 showing heptad WD repeats. Close view of region of interest where C233Y mutation lies. Upper panel shows wild type Wat1 having Cys 233 (colored in red). Lower panel shows model of mutant Wat1 having Tyr at 233 position(colored in red). Images were generated with the help of Chimera1.6. <b>B.</b> The Wat1 mutant protein fails to interact with Prp2 in a yeast two hybrid interaction assay. Prp2 Protein was used as prey, fused with activation domain (pACT2) and the Wat1 or Wat1 mutant protein was fused to the DNA-binding domain (pAS2) as bait. Interaction was analyzed using LacZ as reporter gene on SD-trp-leu plates containing X-gal and HIS marker as a reporter gene on SD-trp-leu plate lacking histidine. 3AT was used to prevent any leaky expression of HIS marker gene.</p

Mapping of <i>wat1-17</i> mutation and its conservation with human Lst8.

<p><b>A.</b> Location of mutation in <i>wat1-17</i> gene. <b>B.</b> ESPript generated sequence alignment of Wat1 and human Lst8. Secondary structure assignment was according to crystal structure Lst8 (PDB-ID, 4JSP).</p

The <i>wat1-17 chk1</i> delete cells shows reduced α tubulin levels and defects in mictrotubule structure.

<p><b>A.</b> The wild type, <i>wat1-17</i> and <i>wat1-17 chk1</i>Δ cells were grown at permissive temperature till mid log phase then shifted at 18°C for indicated time. Protein lysate was prepared as described in material and methods, samples were run on 10% SDS PAGE, transferred on nitrocellulose membrane and probed with anti α-tubulin antibody. Anti-cdc2 antibody was used as loading control. Signals were quantitated on Gel Doc system (Life Technologies) and protein ratio was calculated. The asterisk indicates a non specific band. <b>B.</b> Indicated strains were grown at 25°C and shifted at 18°C for 48 hr. Cells were processed for immunoflourescence microscopy using anti α- tubulin antibody. Scale bar: 10 µm.</p

The diploidisation of <i>wat1-17</i> and <i>wat1-17 chk1Δ</i> strain.

<p><b>A.</b> Wild type, <i>wat1-17</i>, <i>chk1Δ</i> and <i>wat1-17chk1</i>Δ double mutant were grown up to mid log phase, about 1000 cells were spread on YEA plates containing 1.5 µg/ml Phloxine B. All the plates were incubated at 25°C for 3–4 days before taking photographs. <b>B.</b> FACS analysis of wild type, <i>chk1</i>Δ, <i>wat1-17, wat1-17chk1</i>Δ mutants. The asynchronous cultures were grown at 25°C and shifted to 18°C, samples were taken at 12 h interval, fixed and stained with the propidium iodide. Samples were analyzed for BD FACS caliber for DNA content analysis.</p

Strains used in this study.

<p>Strains used in this study.</p

The <i>ts17/wat1-17</i> mutant allele exhibit conditional lethality with <i>chk1</i> knockout.

<p>Indicated strains were grown at 25°C, serially diluted and spotted on YEA plates. Plates were incubated at indicated temperature for 3 days except 18°C plate that was incubated for 7 days before taking photographs.</p

Optical Properties of Zn₂Mo₃O₈: Combination of Theoretical and Experimental Study

We have investigated the electronic structure and optical properties of zinc molybdenum oxide (Zn₂Mo₃O₈) by using both first-principle calculations and experiments. Optical properties of this material is very similar to other ternary oxides of tetravalent molybdenum (A₂Mo₃O₈: A = Mg, Fe, Cd); therefore, this study provides meaningful insight into optical properties and possible phtotovoltaic applicability of these class of metal oxide cluster compounds. We use state-of-the-art methods, based on density functional theory and the GW approximation to the self-energy, to obtain the quasiparticle band structure and absorption spectra of the material. Our calculations shows that Zn₂Mo₃O₈ is a near indirect gap semiconductor with an indirect gap of 3.14 eV. The direct gap of the material is 3.16 eV. We also calculate the optical absorption in the material. Calculated results compare well with UV–visible spectroscopy and spectroscopic ellipsometry measurements done on polycrystalline thin films of Zn₂Mo₃O₈. We show the material has a large excitonic binding energy of 0.78 eV

Reversible Electrochemical Trapping of Carbon Dioxide Using 4,4′-Bipyridine That Does Not Require Thermal Activation

Sequestering carbon dioxide emissions by the trap and release of CO₂ via thermally activated chemical reactions has proven problematic because of the energetic requirements of the release reactions. Here we demonstrate trap and release of carbon dioxide using electrochemical activation, where the reactions in both directions are exergonic and proceed rapidly with low activation barriers. One-electron reduction of 4,4′-bipyridine forms the radical anion, which undergoes rapid covalent bond formation with carbon dioxide to form an adduct. One-electron oxidation of this adduct releases the bipyridine and carbon dioxide. Reversible trap and release of carbon dioxide over multiple cycles is demonstrated in solution at room temperature, and without the requirement for thermal activation

Features of PLAs in the rice genome.

<p>Features of PLAs in the rice genome.</p

Gross and histopathological findings of FMDV-associated myocarditis in still-borne calf.

<p><b>(A)</b> Sanguineous bicavitary effusions in still-borne calf from Dam ID#454. <b>(B)</b> Focal myocarditis seen as area of pallor (arrow) on epicardial surface of heart from aborted calf shown in panel (A). <b>(C)</b> Mixed mononuclear infiltrate and interstitial edema separating myocardial fibers in histological specimen from heart. Hypereosinophilia and loss of striations indicates myofiber degeneration and necrosis. Hematoxylin and Eosin stain. 40x magnification.</p