Anomalous phonon behavior in the high temperature shape memory alloy: TiPd:Cr

Ti50 Pd50-xCrx is a high temperature shape memory alloy with a martensitic transformation temperature strongly dependent on the Cr composition. Prior to the transformation a premartensitic phase is present with an incommensurate modulated cubic lattice with wave vector of q0=(0.22, 0.22, 0). The temperature dependence of the diffuse scattering in the cubic phase is measured as a function temperature for x=6.5, 8.5, and 10 at. %. The lattice dynamics has been studied and reveals anomalous temperature and q-dependence of the [110]-TA2 transverse phonon branch. The phonon linewidth is broad over the entire Brillouin zone and increases with decreasing temperature, contrary to the behavior expected for anharmonicity. No anomaly is observed at q0. The results are compared with first principles calculation of the phonon structure.Comment: 26 pages, 11 figure

Syntaxin of Plant Proteins SYP123 and SYP132 Mediate Root Hair Tip Growth in Arabidopsis thaliana

Root hairs are fast-growing tubular protrusions on root epidermal cells that play important roles in water and nutrient uptake in plants. The tip-focused polarized growth of root hairs is accomplished by the secretion of newly synthesized materials to the tip via the polarized membrane trafficking mechanism. Here, we report the function of two different types of plasma membrane (PM) Qa-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors), SYP123 and SYP132, in the growth of root hair in Arabidopsis. We found that SYP123, but not SYP132, localizes in the tip region of root hairs by recycling between the brefeldin A (BFA)-sensitive endosomes and the PM of the expanding tip in an F-actin-dependent manner. The vesicle-associated membrane proteins VAMP721/722/724 also exhibited tip-focused localization in root hairs and formed ternary SNARE complexes with both SYP123 and SYP132. These results demonstrate that SYP123 and SYP132 act in a coordinated fashion to mediate tip-focused membrane trafficking for root hair tip growth. © 2014 The Author

Mechanisms of Acido-Tolerance and Characteristics of Photosystems in an Acidophilic and Thermophilic Red Alga, Cyanidium Caldarium

In this chapter, we describe the mechanisms of acido-tolerance in an acidophilic- and thermophilic red alga, Cyanidium caldarium. In spite of the extremely acidic environments it inhabits, the intracellular pH of Cyanidium cells is kept neutral by pumping out the protons previously leaked into the cells according to the steep pH gradient. The H+ pump is driven by the plasma membrane ATPase, utilizing intracellular ATP produced by both oxidative phosphorylation and cyclic photophosphorylation via photosystem I. We also describe the characteristics and function of the two photosystems, Photosystem I (PSI) and II (PSII), in Cyanidium caldarium in comparison with those of cyanobacteria, other eukaryotic algae, and higher plants, based on the crystal structures of the two complexes reported so far

Conversion of Iodide to Hypoiodous Acid and Iodine in Aqueous Microdroplets Exposed to Ozone

Halides are incorporated into aerosol sea spray, where they start the catalytic destruction of ozone (O3) over the oceans and affect the global troposphere. Two intriguing environmental problems undergoing continuous research are (1) to understand how reactive gas phase molecular halogens are directly produced from inorganic halides exposed to O3 and (2) to constrain the environmental factors that control this interfacial process. This paper presents a laboratory study of the reaction of O3 at variable iodide (I–) concentration (0.010–100 μM) for solutions aerosolized at 25 °C, which reveal remarkable differences in the reaction intermediates and products expected in sea spray for low tropospheric [O3]. The ultrafast oxidation of I– by O3 at the air–water interface of microdroplets is evidenced by the appearance of hypoiodous acid (HIO), iodite (IO2–), iodate (IO3–), triiodide (I3–), and molecular iodine (I2). Mass spectrometry measurements reveal an enhancement (up to 28%) in the dissolution of gaseous O3 at the gas–liquid interface when increasing the concentration of NaI or NaBr from 0.010 to 100 μM. The production of iodine species such as HIO and I2 from NaI aerosolized solutions exposed to 50 ppbv O3 can occur at the air–water interface of sea spray, followed by their transfer to the gas-phase, where they contribute to the loss of tropospheric ozone

Eukaryotic-like Ser/Thr Protein Kinases SpkC/F/K Are Involved in Phosphorylation of GroES in the Cyanobacterium Synechocystis

Serine/threonine protein kinases (STPKs) are the major participants in intracellular signal transduction in eukaryotes, such as yeasts, fungi, plants, and animals. Genome sequences indicate that these kinases are also present in prokaryotes, such as cyanobacteria. However, their roles in signal transduction in prokaryotes remain poorly understood. We have attempted to identify the roles of STPKs in response to heat stress in the prokaryotic cyanobacterium Synechocystis sp. PCC 6803, which has 12 genes for STPKs. Each gene was individually inactivated to generate a gene-knockout library of STPKs. We applied in vitro Ser/Thr protein phosphorylation and phosphoproteomics and identified the methionyl-tRNA synthetase, large subunit of RuBisCO, 6-phosphogluconate dehydrogenase, translation elongation factor Tu, heat-shock protein GrpE, and small chaperonin GroES as the putative targets for Ser/Thr phosphorylation. The expressed and purified GroES was used as an external substrate to screen the protein extracts of the individual mutants for their Ser/Thr kinase activities. The mutants that lack one of the three protein kinases, SpkC, SpkF, and SpkK, were unable to phosphorylate GroES in vitro, suggesting possible interactions between them towards their substrate. Complementation of the mutated SpkC, SpkF, and SpkK leads to the restoration of the ability of cells to phosphorylate the GroES. This suggests that these three STPKs are organized in a sequential order or a cascade and they work one after another to finally phosphorylate the GroES