对核糖体蛋白S4突变的进一步研究为结构域闭合模型提供了有力支持。
Another look at mutations in ribosomal protein S4 lends strong support to the domain closure model.
作者信息
Fredrick Kurt
机构信息
Department of Microbiology, Ohio State Biochemistry Program, and Center for RNA Biology, Ohio State University, Columbus, Ohio, USA
出版信息
J Bacteriol. 2015 Mar;197(6):1014-6. doi: 10.1128/JB.02579-14. Epub 2014 Dec 29.
Abstract
Ribosomes employ a "kinetic discrimination" mechanism, in which correct substrates are incorporated more rapidly than incorrect ones. The structural basis of this mechanism may involve 30S domain closure, a global conformational change that coincides with codon recognition. In a direct screen for fidelity-altering mutations, Agarwal and coworkers (D. Agarwal, D. Kamath, S. T. Gregory, and M. O'Connor, J Bacteriol 197:1017-1025, 2015, doi:10.1128/JB.02485-14) isolated mutations that progressively truncate the C terminus of S4. All of these promote miscoding and undoubtedly destabilize the S4-S5 interface, consistent with the domain closure model.
摘要
核糖体采用一种“动力学甄别”机制，其中正确的底物比错误的底物掺入速度更快。该机制的结构基础可能涉及30S结构域闭合，这是一种与密码子识别同时发生的全局构象变化。在一项针对改变保真度突变的直接筛选中，阿加瓦尔及其同事（D. 阿加瓦尔、D. 卡马特、S. T. 格雷戈里和M. 奥康纳，《细菌学杂志》197:1017 - 1025，2015，doi:10.1128/JB.02485 - 14）分离出了逐渐截断S4 C末端的突变。所有这些突变都会促进错义编码，并且无疑会破坏S4 - S5界面的稳定性，这与结构域闭合模型一致。
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