The ribosome modulates nascent protein folding.

The ribosome modulates nascent protein folding.
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DOI:
10.1126/science.1209740
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发表时间:
2011-12-23
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Bustamante C
Bustamante C
中科院分区:
其他
文献类型:
--
作者:
Kaiser CM;Goldman DH;Chodera JD;Tinoco I Jr;Bustamante C

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蛋白质由核糖体合成,通常必须折叠才能具有功能活性。尽管人们普遍认为核糖体影响折叠过程,但这一想法极难证明。我们开发了一个实验系统,用光镊研究单个核糖体结合的停滞新生多肽的折叠。在重建的体外翻译系统中合成的 T4 溶菌酶中,核糖体减缓了稳定三级相互作用的形成以及相对于游离蛋白质的天然状态的实现。不完整的 T4 溶菌酶多肽在游离于溶液中时会错误折叠和聚集,但它们在核糖体表面附近仍然具有折叠能力。总而言之,我们的结果表明核糖体不仅解码遗传信息并合成多肽,而且还促进有效地从头获得天然状态。
Proteins are synthesized by the ribosome and generally must fold to become functionally active. Although it is commonly assumed that the ribosome affects the folding process, this idea has been extremely difficult to demonstrate. We have developed an experimental system to investigate the folding of single ribosome-bound stalled nascent polypeptides with optical tweezers. In T4 lysozyme, synthesized in a reconstituted in vitro translation system, the ribosome slows the formation of stable tertiary interactions and the attainment of the native state relative to the free protein. Incomplete T4 lysozyme polypeptides misfold and aggregate when free in solution, but they remain folding-competent near the ribosomal surface. Altogether, our results suggest that the ribosome not only decodes the genetic information and synthesizes polypeptides, but also promotes efficient de novo attainment of the native state.
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