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Kinetic analysis of the m1 RNA folding pathway

机译：m1 RNA折叠途径的动力学分析

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The biological activity of large RNAs is dependent on the formation of complex folded structures that determine function. Typically the creation of such structures requires divalent magnesium and in many cases the folding process takes place over the course of several minutes. It has been proposed that the folding paths of large RNAs proceed through discrete intermediates but the nature of these intermediates is not known in most cases. Here, we describe our studies on the folding of the M1 RNA sub-unit of Escherichia coli RNase P. We performed kinetic footprinting studies of M1 RNA folding with the chemical footprinting reagent peroxynitrous acid to provide a detailed description of the folding pathway of RNase P RNA. Our results indicate that, in contrast to the Group I ribozyme, the M1 RNA folds into its catalytically active structure through the formation of two separately folded domains and that the folding of each proceeds through a discrete series of intermediates. Similar rates of folding were observed for regions believed to form the interface between the two domains. This observation is consistent with a kinetic trap which occurs by interaction of the domains during folding. (C) 2000 Academic Press. [References: 18]
机译：大RNA的生物学活性取决于决定功能的复杂折叠结构的形成。通常，这种结构的产生需要二价镁，并且在许多情况下，折叠过程在几分钟的时间内进行。已经提出，大RNA的折叠路径通过不连续的中间体进行，但是这些中间体的性质在大多数情况下是未知的。在这里，我们描述了我们对大肠杆菌RNase P M1 RNA亚基折叠的研究。我们使用化学足迹试剂过氧亚硝酸对M1 RNA折叠进行了动力学足迹研究，以详细描述RNase P的折叠途径。 RNA。我们的结果表明，与I组核酶相反，M1 RNA通过形成两个单独折叠的域折叠成其催化活性结构，并且每个折叠都通过一系列离散的中间体进行。对于被认为在两个结构域之间形成界面的区域，观察到了相似的折叠速率。该观察结果与通过折叠期间结构域的相互作用而发生的动力学陷阱一致。 （C）2000学术出版社。 [参考：18]

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