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首页> 外文期刊>Biochemistry >The C-Terminal Domain of the Betaine Carrier BetP of Corynebacterium glutamicum Is Directly Involved in Sensing K~+ as an Osmotic Stimulus
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The C-Terminal Domain of the Betaine Carrier BetP of Corynebacterium glutamicum Is Directly Involved in Sensing K~+ as an Osmotic Stimulus

机译：棒状蛋白菌谷氨酰胺的甜菜碱载体BETP的C末端域直接涉及感测K〜+作为渗透刺激

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摘要

The glycine betaine carrier BetP of Corynebacterium glutamicum was recently shown to function both as an osmosensor and as an osmoregulator in proteoliposomes by sensing changes in the internal K~+ concentration as a measure of hyperosmotic stress.In vivo analysis of mutants carrying deletions at the C-terminal extension of BetP indicated that this domain participates in osmostress-dependent activity regulation.To address the question,whether a putative K~+ sensor is located within the C-terminal domain,several mutants with truncations in this domain were purified and reconstituted in proteoliposomes of Escherichia coli phospholipids,since this in vitro system allowed variation of the K~+ concentration at the lumenal side.Truncation of 12 amino acids led to a partly deregulated BetP in terms of osmoregulation;however,K~+ sensitivity was not impaired in this mutant.The deletion of 25 amino acid residues at the C-terminal end of BetP led to both deregulation of the carrier activity,i.e.,high activity independent of external osmolality,and loss of K~+-dependent transport stimulation,indicating that this region of the C-terminal domain is necessary for K~+ sensing and/or K~+-dependent carrier activation.Immunological and proteolysis analyses showed that BetP and its recombinant forms were reconstituted in a right-side-out orientation,i.e.,the C-terminal domain faces the lumen of the proteoliposomes and is thus able to detect the K~+ signal at the inside.This is the first experimental demonstration of a direct connection between an osmotic stimulus,i.e.,the change in internal K~+,and a putative sensor domain.
机译：最近显示甘氨酸甜菜碱载体的糖氨基氨基甲酰胺载体β通过作为蛋白质体在蛋白质体中的Osmoreculator，通过感测内部K〜+浓度的变化，作为蛋白质体的Osmoreculator，作为血管染色胁迫的量度。在C脱裂的突变体的体内分析BETP的终端延伸表明该域参与Osmostress依赖的活动调节。要解决问题，是否推定的K〜+传感器位于C末端域内，纯化并重建该结构域中截短的几个突变体大肠杆菌磷脂的蛋白聚体，因为该体外系统允许腔侧的K〜+浓度的变化。在Osmoreculation方面，将12个氨基酸的条纹LED导致部分令人讨来的β;但是，K〜+敏感性不会受到损害该突变体。在BETP的C末端的25个氨基酸残基的缺失导致载体活性的放松管制，即高活性独立于外部渗透压，并且丧失K〜+依赖性运输刺激，表明C-末端域的该区域是K〜+感测和/或K〜+依赖性载体激活所必需的.immunology和蛋白水解分析表明，在右侧取向方向上重构BETP及其重组形式，即C末端域面对蛋白质面体的内腔，因此能够检测内部的K +信号。这是第一个渗透刺激之间直接连接的实验证明，即内部k〜+的变化和推定的传感器结构域。

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  • 来源
    《Biochemistry》 |2004年第19期|共9页
  • 作者

    Dirk Schiller; Rene Rubenhagen; Reinhard Kramer; Susanne Morbach;

  • 作者单位

    Institut fur Biochemie der Universitdt zu Koln Zulpicher Strasse 47 50674 Koln Germany and GBF-Gesellschaft fur Biotechnologische Forschung mbH Mascheroder Weg 1 38124 Braunschweig Germany;

    Institut fur Biochemie der Universitdt zu Koln Zulpicher Strasse 47 50674 Koln Germany and GBF-Gesellschaft fur Biotechnologische Forschung mbH Mascheroder Weg 1 38124 Braunschweig Germany;

    Institut fur Biochemie der Universitdt zu Koln Zulpicher Strasse 47 50674 Koln Germany and GBF-Gesellschaft fur Biotechnologische Forschung mbH Mascheroder Weg 1 38124 Braunschweig Germany;

    Institut fur Biochemie der Universitdt zu Koln Zulpicher Strasse 47 50674 Koln Germany and GBF-Gesellschaft fur Biotechnologische Forschung mbH Mascheroder Weg 1 38124 Braunschweig Germany;

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  • 中图分类 生物化学;
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