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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Contribution of cotranslational folding to the rate of formation of native protein structure.
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Contribution of cotranslational folding to the rate of formation of native protein structure.

机译：共翻译折叠对天然蛋白质结构形成速率的贡献。

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摘要

To compare the process of protein folding in the cell with refolding following denaturation in vitro, we have investigated and compared the kinetics of renaturation of a full-length protein upon dilution from concentrated urea with the rate of folding in the course of biosynthesis. Formation of enzymatically active bacterial luciferase, an alpha beta heterodimer, occurred 2 min after completion of beta-subunit synthesis in an Escherichia coli cell-free system. Renaturation of urea-denatured beta subunit, either in the presence of the cell-free protein synthesis system or in buffer solutions, proceeded more slowly. Cellular components present in the cell-free protein synthesis system slightly accelerated the rate of refolding of urea-unfolded beta subunit. The results indicate that the luciferase beta subunit begins the folding process cotranslationally and that cotranslational folding contributes to the rapid formation of the native structure in the cell.
机译：为了比较体外变性后细胞中蛋白质折叠和再折叠的过程，我们研究并比较了从浓缩尿素稀释后全长蛋白质复性的动力学和生物合成过程中的折叠速率。酶活性细菌荧光素酶（一种αβ异二聚体）的形成在无细胞大肠杆菌系统中完成β亚基合成后2分钟发生。在无细胞蛋白质合成系统的存在下或在缓冲溶液中，尿素变性的β亚基的复性过程进行得较慢。无细胞蛋白质合成系统中存在的细胞成分略微加快了尿素展开的β亚基的重折叠速度。结果表明，萤光素酶β亚基共翻译开始折叠过程，并且共翻译折叠有助于细胞中天然结构的快速形成。

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