Structure of ribonuclease P--a universal ribozyme.

Abstract:

:Ribonuclease P (RNase P) is one of only two known universal ribozymes and was one of the first ribozymes to be discovered. It is involved in RNA processing, in particular the 5' maturation of tRNA. Unlike most other natural ribozymes, it recognizes and cleaves its substrate in trans. RNase P is a ribonucleoprotein complex containing one RNA subunit and as few as one protein subunit. It has been shown that, in bacteria and in some archaea, the RNA subunit alone can support catalysis. The structure and function of bacterial RNase P RNA have been studied extensively, but the detailed catalytic mechanism is not yet fully understood. Recently, structures of one of the structural domains and of the entire RNA component of RNase P from two different bacteria have been described. These structures provide the first atomic-level information on the structural assembly of the RNA component, and the regions involved in substrate recognition and catalysis. Comparison of these structures reveals a highly conserved core that comprises two universally conserved structural modules. Interestingly, the same structural core can be found in the context of different scaffolds.

journal_name

Curr Opin Struct Biol

authors

Torres-Larios A,Swinger KK,Pan T,Mondragón A

doi

10.1016/j.sbi.2006.04.002

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

327-35

issue

3

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(06)00066-2

journal_volume

16

pub_type

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