Kinetic analysis of the m1 RNA folding pathway

被引:22
作者
Kent, O
Chaulk, SG
MacMillan, AM
机构
[1] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2C6, Canada
[2] Univ Toronto, Dept Chem, Toronto, ON M5S 3H6, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
RNase P; M1; RNA; peroxynitrous acid; kinetic footprinting; RNA folding;
D O I
10.1006/jmbi.2000.4263
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:699 / 705
页数:7
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