Finite temperature properties of the two-dimensional SU(2) Kondo-necklace

We analyse several thermodynamic properties of the two-dimensional Kondo necklace using finite-temperature stochastic series expansion. In agreement with previous zero-temperature findings the model is shown to exhibit a quantum critical point (QCP), separating an antiferromagnetic from a paramagnetic dimerized state at a critical Kondo exchange-coupling strength $J_{c}\approx 1.4$. We evaluate the temperature dependent uniform and staggered structure factors as well as the uniform and staggered susceptibilities and the local 'impurity' susceptibility close to the QCP as well as in the ordered and quantum disordered phase. The crossover between the classical, renormalized classical, and quantum critical regime is analyzed as a function of temperature and Kondo coupling.Comment: 4.2 pages, 6 figure

Feeding on leaves of the glucosinolate transporter mutant <i>gtr1gtr2 </i>reduces fitness of <i>Myzus persicae</i>

As aphids are a pest on various crops worldwide, a better understanding of the interaction between aphids and plant host defenses is required. The green peach aphid (Myzus persicae) feeds on a variety of plant species, including the model plant Arabidopsis thaliana (Arabidopsis), in which glucosinolates function as a major part of the chemical defense. Several studies have shown that glucosinolates play a role in interactions between Arabidopsis and the green peach aphid. In this work, we used a recently identified Arabidopsis glucosinolate transporter mutant (gtr1gtr2 dKO), with altered glucosinolate content in the vasculature, to investigate the role of defense compound transport in aphid infestation. By monitoring aphid performance on caged leaves and analyzing glucosinolates in leaf tissue and phloem sap, as well as inside aphids, we examined if a change in spatial distribution of glucosinolates within a leaf influences aphid performance. Based on reduced glucosinolate content in the phloem sap of the transporter mutant, we hypothesized that aphids would perform better on gtr1gtr2 dKO leaves compared to WT. Unexpectedly, aphids performed poorly on gtr1gtr2 dKO leaves. Our data suggest that higher glucosinolate content in tissues surrounding the phloem of the double transporter mutant may play a role in reducing aphid performance on this genotype. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10886-015-0641-3) contains supplementary material, which is available to authorized users

Optimization of engineered production of the glucoraphanin precursor dihomomethionine in <i>Nicotiana benthamiana</i>

Glucosinolates are natural products characteristic of the Brassicales order, which include vegetables such as cabbages and the model plant Arabidopsis thaliana. Glucoraphanin is the major glucosinolate in broccoli and associated with the health-promoting effects of broccoli consumption. Toward our goal of creating a rich source of glucoraphanin for dietary supplements, we have previously reported the feasibility of engineering glucoraphanin in Nicotiana benthamiana through transient expression of glucoraphanin biosynthetic genes from A. thaliana (Mikkelsen et al., 2010). As side-products, we obtained fivefold to eightfold higher levels of chain-elongated leucine-derived glucosinolates, not found in the native plant. Here, we investigated two different strategies to improve engineering of the methionine chain elongation part of the glucoraphanin pathway in N. benthamiana: (1) coexpression of the large subunit (LSU1) of the heterodimeric isopropylmalate isomerase and (2) coexpression of BAT5 transporter for efficient transfer of intermediates across the chloroplast membrane. We succeeded in raising dihomomethionine (DHM) levels to a maximum of 432 nmol g(−1) fresh weight that is equivalent to a ninefold increase compared to the highest production of this intermediate, as previously reported (Mikkelsen et al., 2010). The increased DHM production without increasing leucine-derived side-product levels provides new metabolic engineering strategies for improved glucoraphanin production in a heterologous host