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The enigma of ribonuclease P evolution
Enno Hartmann1, Roland K Hartmann
1Institut für Biologie, Universität zu Lübeck, Ratzeburger Allee 160, D-23538, Lübeck, Germany. roland.hartmann@staff.uni-marburg.de
Trends in Genetics : TIG
|October 11, 2003
Summary
Ribonuclease P (RNase P) protein subunit evolution reveals Pop4 is conserved across Eukarya and Archaea. Bacterial and archaeal-eukaryotic RNase P proteins lack structural homology, suggesting divergent evolutionary paths.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Ribonuclease P (RNase P) is essential for tRNA 5'-end maturation in all domains of life.
- RNase P is a ribonucleoprotein enzyme, composed of RNA and protein subunits.
Purpose of the Study:
- To provide a comprehensive overview of RNase P protein homologs in Eukarya and Archaea.
- To investigate the evolutionary history and subunit composition of RNase P across different domains.
Main Methods:
- Bioinformatic analysis of available genome sequences.
- Comparative analysis of RNase P protein subunit representation.
Main Results:
- Most eukaryotes possess homologs for the four archaeal RNase P protein subunits (Pop4, Rpp1, Pop5, Rpr2).
- Pop4 is the sole RNase P protein subunit found in all analyzed Eukarya and Archaea.
- No structural homology exists between bacterial and archaeal-eukaryotic RNase P proteins.
Conclusions:
- RNase P likely originated as an 'RNA-alone' enzyme.
- Progenitors of Bacteria and Archaea diverged early, independently acquiring protein subunits.
- This led to distinct strategies in evolving the RNA-protein state of RNase P.
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