共 1 条
- [1] 3′-end processing of precursor M1 RNA by the N-terminal half of RNase EFEBS LETTERS, 2002, 529 (2-3): : 225 - 231Sim, SKim, KSLee, Y
Kinetic analysis of precursor M1 RNA molecules for exploring substrate specificity of the N-terminal catalytic half of RNase E
被引：3
作者：
Kim, KS
Sim, S
Ko, JH
Cho, B
Lee, Y
[1
]
机构：
[1] Korea Adv Inst Sci & Technol, Dept Chem, Taejon 305701, South Korea
[2] Korea Adv Inst Sci & Technol, Ctr Mol Design & Synth, Taejon 305701, South Korea
[3] Chongju Univ, Dept Chem, Chonju 360764, South Korea
关键词：
parameters;
M1;
RNA;
RNase e;
rne-dependent site;
substrate specificity;
D O I：
10.1093/jb/mvh176
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：
To gain insight into the mechanism by which the sequence at the rne-dependent site of substrate RNA affects the substrate specificity of Escherichia coli RNase E, we performed kinetic analysis of the cleavage of precursor M1 RNA molecules containing various sequences at the rne-dependent site by the N-terminal catalytic half of RNase E (NTH-RNase E). NTH-RNase E displayed higher K-m and k(cat) values for more specific substrates. The retention of single strandedness at the rne-dependent site was essential for cleavage efficiency. Moreover, the loss of single-strandedness was accompanied by a decrease in both the K-m and k(eat) values.
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页码：693 / 699
页数：7
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