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首页> 外文期刊>Biochemistry >Phosphorylation of Thellungiella salsuginea Dehydrins TsDHN-1 and TsDHN-2 Facilitates Cation-Induced Conformational Changes and Actin Assembly
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Phosphorylation of Thellungiella salsuginea Dehydrins TsDHN-1 and TsDHN-2 Facilitates Cation-Induced Conformational Changes and Actin Assembly

机译：Thellungiella salsuginea脱氢Tsdhn-1和Tsdhn-2的磷酸化促进了阳离子诱导的构象变化和肌动蛋白组件

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摘要

Group 2 late embryogenesis abundant (LEA) proteins, also known as dehydrins, are intrinsically disordered proteins that are expressed in plants experiencing extreme environmental conditions such as drought or low temper-atures. These proteins are characterized by the presence of at least one conserved, lysine-rich K-segment and sometimes by one or more serine-rich S-segments that are phosphorylated. Dehydrins may stabilize proteins and membrane structures during environmental stress and can sequester and scavenge metal ions. Here. we investigate how the conformations of two dehydrins from Thellungiella salsuginea, denoted as TsDHN-1 (acidic) and TsDHN-2 (basic), are affected by pH, interactions with cations and membranes, and phosphorylation. Both TsDHN-1 and TsDHN-2 were expressed as SUMO fusion proteins for in vitro phosphorylation by casein kinase H (CKII), and structural analysis by circular dichroism and attenuated total reflection-Fourier transform infrared spectroscopy. We show that the polyproline II conformation can be induced in the dehydrins by their environmental conditions, including changes in the concentration of divalent cations such as Ca~(2+). The assembly of actin by these dehydrins was assessed by sedimentation assays and viewed by transmission electron and atomic force microscopy. Phosphorylation allowed both dehydrins to polymerize actin filaments. These results support the hypothesis that dehydrins stabilize the cytoskeleton under stress conditions and further that phosphorylation may be an important feature of this stabilization.
机译：第2组晚期胚胎发生丰富（LEA）蛋白，也称为脱氢，是本质上无序的蛋白质，其在经历极端的环境条件如干旱或低发脾气的植物中表达。这些蛋白质的特征在于存在至少一种保守的赖氨酸富含k段，有时是由磷酸化的一种或多种富含丝氨酸的S段。脱氢可以在环境应激期间稳定蛋白质和膜结构，并可以螯合和清除金属离子。这里。我们调查来自Thellungiella Salsuginea的两种脱氢的构象如何，表示为TSDHN-1（酸性）和TSDHN-2（碱性），受到pH，与阳离子和膜的相互作用的影响，以及磷酸化。 TSDHN-1和TSDHN-2都表示为SUMO融合蛋白，用于通过酪蛋白激酶H（CKII）的体外磷酸化，以及通过圆形二色性和衰减的总反射 - 傅里叶变换红外光谱分子的结构分析。我们表明，聚丙烯II构象可以通过它们的环境条件在脱氢中诱导，包括少数阳离子如Ca〜（2+）的变化。通过沉淀测定评估这些脱水的肌动蛋白的组装，并通过透射电子和原子力显微镜观察。磷酸化允许脱氢可聚合肌动蛋白长丝。这些结果支持脱氢裂解在应力条件下稳定细胞骨架的假设，进一步磷酸化可能是这种稳定化的重要特征。

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  • 来源
    《Biochemistry》 |2011年第44期|共18页
  • 作者

    Luna N. Rahman; Graham S. T. Smith; Vladimir V. Bamm; Janine A. M. Voyer-Grant; Barbara A. Moffatt; John R Dutcher; George Harauz;

  • 作者单位

    Department of Molecular and Cellular Biology University of Guelph Guelph ON N1G 2W1 Canada;

    Department of Molecular and Cellular Biology University of Guelph Guelph ON N1G 2W1 Canada;

    Department of Molecular and Cellular Biology University of Guelph Guelph ON N1G 2W1 Canada;

    Department of Molecular and Cellular Biology University of Guelph Guelph ON N1G 2W1 Canada;

    Department of Biology University of Waterloo Waterloo ON N2L 3G1 Canada;

    Department of Physics University of Guelph Guelph ON NIG 2W1 Canada;

    Department of Molecular and Cellular Biology University of Guelph Guelph ON N1G 2W1 Canada;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

    Phosphorylation; Changes; Assembly;

    机译：磷酸化;变化;组装;

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