Nuclear-localized subtype of end-binding 1 protein regulates spindle organization in Arabidopsis

End-binding 1 (EB1) proteins are evolutionarily conserved plus-end-tracking proteins that localize to growing microtubule plus ends where they regulate microtubule dynamics and interactions with intracellular targets. Animal EB1 proteins have acidic C-terminal tails that might induce an autoinhibitory conformation. Although EB1 proteins with the same structural features occur in plants (EB1a and EB1b in Arabidopsis thaliana), a variant form (EB1c) is present that lacks the characteristic tail. We show that in Arabidopsis the tail region of EB1b, but not of EB1c, inhibits microtubule assembly in vitro. EB1a and EB1b form heterodimers with each other, but not with EB1c. Furthermore, the EB1 genes are expressed in various cell types of Arabidopsis, but the expression of EB1c is particularly strong in the meristematic cells where it is targeted to the nucleus by a nuclear localization signal in the C-terminal tail. Reduced expression of EB1c compromised the alignment of spindle and phragmoplast microtubules and caused frequent lagging of separating chromosomes at anaphase. Roots of the eb1c mutant were hypersensitive to a microtubule-disrupting drug and complete rescue of the mutant phenotype required the tail region of EB1c. These results suggest that a plant-specific EB1 subtype has evolved to function preferentially on the spindle microtubules by accumulating in the prophase nucleus

Drell-Yan Production of Z' in the Three-Site Higgsless Model at the LHC

In the Higgsless models, there are extra gauge bosons which keep the perturbative unitarity of a longitudinally polarized gauge boson. The three-site Higgsless model is a minimal Higgsless model and contains three extra gauge bosons, $W^{\prime \pm}$ and Z'. In this paper, we report the discovery potential of the Z' gauge boson via Drell-Yan production with Z'(mass=380, 500, 600 GeV) $\rightarrow WW \rightarrow \ell\nu qq$ ($\ell=e$, $\mu$) at the LHC ($\sqrt{s}$=14 TeV).Comment: 7 pages, 5 figures included. References revise

Geometry of Peterson Schubert calculus in type A and left-right diagrams

We introduce an additive basis of the integral cohomology ring of the Peterson variety which reflects the geometry of certain subvarieties of the Peterson variety. We explain the positivity of the structure constants from a geometric viewpoint, and provide a manifestly positive combinatorial formula for them. We also prove that our basis coincides with the additive basis introduced by Harada-Tymoczko.Comment: 29 page

市場メカニズムを活用した地球温暖化対策の政策効果に関する実証研究

早大学位記番号:新9178博士(経済学)早稲田大

Water-in-CO2 Microemulsions Stabilized by an Efficient Catanionic Surfactant

To facilitate potential applications of water-in-supercritical CO2 microemulsions (W/CO2 μEs) efficient and environmentally responsible surfactants are required with low levels of fluorination. As well as being able to stabilize water–CO2 interfaces, these surfactants must also be economical, prevent bioaccumulation and strong adhesion, deactivation of enzymes, and be tolerant to high salt environments. Recently, an ion paired catanionic surfactant with environmentally acceptable fluorinated C6 tails was found to be very effective at stabilizing W/CO2 μEs with high water-to-surfactant molar ratios (W0) up to ∼50 (Sagisaka, M.; et al. Langmuir 2019, 35, 3445−3454). As the cationic and anionic constituent surfactants alone did not stabilize W/CO2 μEs, this was the first demonstration of surfactant synergistic effects in W/CO2 microemulsions. The aim of this new study is to understand the origin of these intriguing effects by detailed investigations of nanostructure in W/CO2 microemulsions using high-pressure small-angle neutron scattering (HP-SANS). These HP-SANS experiments have been used to determine the headgroup interfacial area and volume, aggregation number, and effective packing parameter (EPP). These SANS data suggest the effectiveness of this surfactant originates from increased EPP and decreased hydrophilic/CO2-philic balance, related to a reduced effective headgroup ionicity. This surfactant bears separate C6F13 tails and oppositely charged headgroups, and was found to have a EPP value similar to that of a double C4F9-tail anionic surfactant (4FG(EO)2), which was previously reported to be one of most efficient stabilizers for W/CO2 μEs (maximum W0 = 60–80). Catanionic surfactants based on this new design will be key for generating superefficient W/CO2 μEs with high stability and water solubilization

Membrane hyperpolarization and depolarization of rat thymocytes by azoxystrobin, a post harvest fungicide

Azoxystrobin, a broad-spectrum fungicide, has been increasingly used in the agricultural industry. In Japan in 2018, azoxystrobin at five times the normal limit was detected in a shipment of Australian barley that had been used in food products. Therefore, the effects of azoxystrobin need to be carefully examined to predict potential adverse reactions in humans. In this study, the effects of azoxystrobin on the membrane potential and intracellular Ca2+ levels of thymocytes have been photochemically examined using flow cytometry. Azoxystrobin hyperpolarized plasma membrane potential. This hyperpolarization appeared to be due to the activation of Ca2+-dependent K+ channels, as both the removal of extracellular Ca2+ and addition of charybdotoxin attenuated the observed hyperpolarization. In the presence of quinine, an anti-malarial drug that blocks Ca2+-dependent K+ channels, azoxystrobin depolarized the membranes instead. Azoxystrobin increased intracellular Ca2+ levels in a concentration-dependent manner through the influx of extracellular Ca2+ and intracellular release of Ca2+, as confirmed by reduction in azoxystrobin-induced response in the absence of extracellular Ca2+. It appears likely that azoxystrobin at micromolar concentrations modifies membrane ion permeability in thymocytes. Since changes in membrane potential and intracellular Ca2+ levels occur during typical physiological lymphocyte responses, azoxystrobin may disturb lymphocyte function