Ribonuclease P: the diversity of a ubiquitous RNA processing enzyme.

Abstract:

:Ribonuclease P is the endonuclease required for generating the mature tRNA 5'-end. The ribonucleoprotein character of this enzyme has now been proven in most organisms and organelles. Exceptions, however, are still the chloroplasts, plant nuclei and animal mitochondria where no associated RNAs have been detected to date. In contrast to the known RNA subunits, which are fairly well-conserved in size and structure among diverse phylogenetic groups, the protein contribution to the holoenzyme is highly variable in size and number of the individual components. The structure of the bacterial protein component has recently been solved. In contrast, the spatial arrangement of the multiple subunits in eukaryotic enzymes is still enigmatic. Substrate requirements of the enzymes or their catalytic RNA subunits are equally diverse, ranging from simple single domain mimics to an almost intact three-dimensional structure of the pre-tRNA substrate. As an example for an intermediate in the enzyme evolution, ribonuclease P from the Cyanophora paradoxa cyanelle will be discussed in more detail. This enzyme is unique, as it combines cyanobacterial and eukaryotic features in its function, subunit composition and holoenzyme topology.

journal_name

FEMS Microbiol Rev

authors

Schön A

doi

10.1111/j.1574-6976.1999.tb00406.x

subject

Has Abstract

pub_date

1999-06-01 00:00:00

pages

391-406

issue

3

eissn

0168-6445

issn

1574-6976

pii

S0168-6445(99)00014-5

journal_volume

23

pub_type

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