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首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >Protein cold adaptation strategy via a unique seven-amino acid domain in the icefish (Chionodraco hamatus) PEPT1 transporter
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Protein cold adaptation strategy via a unique seven-amino acid domain in the icefish (Chionodraco hamatus) PEPT1 transporter

机译：通过冰鱼（Chionodraco hamatus）PEPT1转运蛋白中独特的七个氨基酸结构域的蛋白质冷适应策略

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Adaptation of organisms to extreme environments requires proteins to work at thermodynamically unfavorable conditions. To adapt to subzero temperatures, proteins increase the flexibility of parts of, or even the whole, 3D structure to compensate for the lower thermal kinetic energy available at low temperatures. This may be achieved through single-site amino acid substitutions in regions of the protein that undergo large movements during the catalytic cycle, such as in enzymes or transporter proteins. Other strategies of cold adaptation involving changes in the primary amino acid sequence have not been documented yet. In Antarctic icefish (Chionodraco hamatus) peptide transporter 1 (PEPT1), the first transporter cloned from a vertebrate living at subzero temperatures, we came upon a unique principle of cold adaptation. A de novo domain composed of one to six repeats of seven amino acids (VDMSRKS), placed as an extra stretch in the cytosolic COOH-terminal region, contributed per se to cold adaptation. VDMSRKS was in a protein region uninvolved in transport activity and, notably, when transferred to the COOH terminus of a warm-adapted (rabbit) PEPT1, it conferred cold adaptation to the receiving protein. Overall, we provide a paradigm for protein cold adaptation that relies on insertion of a unique domain that confers greater affinity and maximal transport rates at low temperatures. Due to its ability to transfer a thermal trait, the VDMSRKS domain represents a useful tool for future cell biology or biotechnological applications.
机译：要使生物适应极端环境，就需要蛋白质在热力学不利条件下起作用。为了适应零度以下的温度，蛋白质可提高部分3D结构甚至整个3D结构的柔韧性，以补偿低温下可用的较低热动能。这可以通过在催化循环中经历大运动的蛋白质区域中的单位氨基酸取代来实现，例如在酶或转运蛋白中。尚未涉及涉及一级氨基酸序列变化的其他冷适应策略。在南极冰鱼（Chionodraco hamatus）肽转运蛋白1（PEPT1）中，这是从生活在零度以下温度的脊椎动物中克隆的第一个转运蛋白，我们经历了冷适应的独特原理。由七个氨基酸的一到六个重复组成的从头结构域（VDMSRKS）作为胞质COOH末端区域的额外片段，本身就对冷适应做出了贡献。 VDMSRKS位于蛋白区域，不涉及转运活性，尤其是当转移到温暖适应的（兔）PEPT1的COOH末端时，VDMSRKS赋予了对接收蛋白的冷适应性。总的来说，我们为蛋白质冷适应提供了一个范式，它依赖于插入一个独特的域，该域在低温下具有更大的亲和力和最大的转运速率。由于其传递热性状的能力，VDMSRKS域代表了未来细胞生物学或生物技术应用的有用工具。

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