Kinetic analysis of precursor M1 RNA molecules for exploring substrate specificity of the N-terminal catalytic half of RNase E.

Abstract:

: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(cat) values.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kim KS,Sim S,Ko JH,Cho B,Lee Y

doi

10.1093/jb/mvh176

keywords:

subject

Has Abstract

pub_date

2004-11-01 00:00:00

pages

693-9

issue

5

eissn

0021-924X

issn

1756-2651

pii

136/5/693

journal_volume

136

pub_type

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