Ribonuclease P: the diversity of a ubiquitous RNA processing enzyme

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...

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Bibliographic Details
Published in:FEMS microbiology reviews 1999-06, Vol.23 (3), p.391-406
Main Author: Schon, A
Format: Article
Language:English
Subjects:
Animals
Base Sequence
Cyanophora paradoxa
Cyanophyta
Endoribonucleases - chemistry
Endoribonucleases - genetics
Endoribonucleases - metabolism
Eukaryote
Evolution
Humans
Mitochondria - enzymology
Models, Molecular
Molecular Sequence Data
Organelle
Plastids - enzymology
Pre-tRNA processing
Protein Conformation
Ribonuclease P
Ribozyme
RNA, Archaeal - metabolism
RNA, Bacterial - metabolism
RNA, Catalytic - chemistry
RNA, Catalytic - genetics
RNA, Catalytic - metabolism
RNA, Transfer - metabolism
Space life sciences
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Summary: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.
ISSN:0168-6445
1574-6976
DOI:10.1016/S0168-6445(99)00014-5