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Cleavage mediated by the catalytic domain of bacterial RNase P RNA.

Abstract：

:Like other RNA molecules, RNase P RNA (RPR) is composed of domains, and these have different functions. Here, we provide data demonstrating that the catalytic (C) domain of Escherichia coli (Eco) RPR when separated from the specificity (S) domain mediates cleavage using various model RNA hairpin loop substrates. Compared to full-length Eco RPR, the rate constant, k(obs), of cleavage for the truncated RPR (CP RPR) was reduced 30- to 13,000-fold depending on substrate. Specifically, the structural architecture of the -1/+73 played a significant role where a C(-1)/G(+73) pair had the most dramatic effect on k(obs). Substitution of A(248) (E. coli numbering), positioned near the cleavage site in the RNase P-substrate complex, with G in the CP RPR resulted in 30-fold improvement in rate. In contrast, strengthening the interaction between the RPR and the 3' end of the substrate only had a modest effect. Interestingly, although deleting the S-domain gave a reduction in the rate, it resulted in a less erroneous RPR with respect to cleavage site selection. These data support and extend our understanding of the coupling between the distal interaction between the S-domain and events at the active site. Our findings will also be discussed with respect to the structure of RPR derived from different organisms.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Wu S,Kikovska E,Lindell M,Kirsebom LA

doi

10.1016/j.jmb.2012.05.020

subject

Has Abstract

pub_date

2012-09-14 00:00:00

pages

204-14

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(12)00405-6

journal_volume

422

pub_type

杂志文章

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