23 research outputs found

    A TSPO-related protein localizes to the early secretory pathway in Arabidopsis, but is targeted to mitochondria when expressed in yeast

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    AtTSPO is a TspO/MBR domain-protein potentially involved in multiple stress regulation in Arabidopsis. As in most angiosperms, AtTSPO is encoded by a single, intronless gene. Expression of AtTSPO is tightly regulated both at the transcriptional and post-translational levels. It has been shown previously that overexpression of AtTSPO in plant cell can be detrimental, and the protein was detected in the endoplasmic reticulum (ER) and Golgi stacks, contrasting with previous findings and suggesting a mitochondrial subcellular localization for this protein. To ascertain these findings, immunocytochemistry and ABA induction were used to demonstrate that, in plant cells, physiological levels of AtTSPO colocalized with AtArf1, a mainly Golgi-localized protein in plant cells. In addition, fluorescent protein-tagged AtTSPO was targeted to the secretory pathway and did not colocalize with MitoTracker-labelled mitochondria. These results suggest that the polytopic membrane protein AtTSPO is cotranslationally targeted to the ER in plant cells and accumulates in the Trans-Golgi Network. Heterologous expression of AtTSPO in Saccharomyces cerevisiae, yeast devoid of TSPO-related protein, resulted in growth defects. However, subcellular fractionation and immunoprecipitation experiments showed that AtTSPO was targeted to mitochondria where it colocalized and interacted with the outer mitochondrial membrane porin VDAC1p, reminiscent of the subcellular localization and activity of mammalian translocator protein 18 kDa TSPO. The evolutionarily divergent AtTSPO appears therefore to be switching its sorting mode in a species-dependent manner, an uncommon peculiarity for a polytopic membrane protein in eukaryotic cells. These results are discussed in relation to the recognition and organelle targeting mechanisms of polytopic membrane proteins in eukaryotic cells

    Uranium mobility in organic matter-rich sediments: A review of geological and geochemical processes

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    Uranium (U) is of enormous global importance because of its use in energy generation, albeit with potential environmental legacies. While naturally occurring U is widespread in the Earth's crust at concentrations of ~1 to 3 ppm, higher concentrations can be found, includingwithin organicmatter (OM)-rich sediments, leading to economic extraction opportunities. The primary determinants of U behaviour in ore systems are pH, Eh, U oxidation state (U(IV), U(VI)) and the abundance of CO3 2– ions. The concentration/availability and interrelationships among such determinants vary, and the solubility and mobility of ions (e.g. OH-, CO3 2–, PO4 3-, SiO4 4-, SO4 2-) that compete for U (primarily as U(VI)) will also influence the mobility of U. In addition, the presence of OM can influence U mobility and fate by the degree of OMsorption to mineral surfaces (e.g. Fe- and Si- oxides and hydroxides). Within solid-phase OM, microbes can influence U oxidation state and U stability through direct enzymatic reduction, biosorption, biomineralisation and bioaccumulation. The biogenic UO2 product is, however, reported to be readily susceptible to reoxidation and therefore more likely remobilised over longer time periods. Thus several areas of uncertainty remain with respect to factors contributing to U accumulation, stability and/or (re)mobilisation. To address these uncertainties, this paper reviews U dynamics at both geological and molecular scales. Here we identify U-OMbond values that are in agreement, relatively strong, independent from ionic strength and which may facilitate either U mobilisation or immobilisation, depending on environmental conditions. We also examine knowledge gaps in the literature, with U-OM solubility data generally lacking in comparison to data for U sorption and dissolution, and little information available on multi-component relationships, such as UOM-V (V as vanadate). Furthermore, the capability ofOMto influence the oxidation state of U at near surface conditions remains unclear, as it can be postulated that electron shuttling by OM may contribute to changes in U redox state otherwise mediated by bacteria. Geochemical modelling of the environmental mobility of U will require incorporation of data from multi-corporation studies, as well as from studies of U-OM microbial interactions, all of which are considered in this review

    EVALUATION DES PRATIQUES (LE LEPONEX* AU CENTRE HOSPITALIER DE RAVENEL)

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    NANCY1-SCD Pharmacie-Odontologie (543952101) / SudocSudocFranceF

    A physical map of large segments of pig chromosome 7q11-q14: comparative analysis with human chromosome 6p21.

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    Chantier qualité spécifique "Auteurs Externes" département de Génétique animale : uniquement liaison auteur au référentiel HR-AccessInternational audienc

    Rapid responses to steroid hormones: from frog skin to human colon. A homage to Hans Ussing

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    AbstractFifty years ago, Hans Ussing described the mechanism by which ions are actively transported across frog skin. Since then, an enormous amount of effort has been invested in determining the cellular and molecular specifics of the transport mechanisms and their regulatory pathways. Ion transport in high-resistance epithelia is regulated by a variety of hormonal and non-hormonal factors. In vertebrates, steroid hormones such as mineralocorticoids, glucocorticoids and estrogens are major regulators of ion and water transport and hence are central to the control of extracellular fluid volume and blood pressure. Steroid hormones act through nuclear receptors to control the transcriptional activity of specific target genes, such as ion channels, ion transporters and ion pumps. These effects are observed after a latency of several hours and can last for days leading to cellular differentiation that allows a higher transport activity. This pathway is the so-called genomic phase. However, in the past 10 years, it has become apparent that steroid hormones can regulate electrolyte and water transport in tight epithelia independently of the transcription of these ion channels and transporters by regulating ion transporter activity in a non-genomic fashion via modulation of various signal transduction pathways. The molecular mechanisms underlying the steroid hormone-induced activation of signal transduction pathways such as protein kinase C (PKC), protein kinase A (PKA), intracellular calcium, intracellular pH and mitogen-activated protein kinases (MAPKs) and how non-genomic activation of these pathways influences epithelial ion transport will be discussed in this review
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