| Literature DB >> 26341299 |
Marcus Lechner1, Walter Rossmanith2, Roland K Hartmann1, Clemens Thölken1, Bernard Gutmann3, Philippe Giegé4, Anthony Gobert4.
Abstract
RNase P is the endonuclease that removes 5' leader sequences from tRNA precursors. In Eukarya, separate RNase P activities exist in the nucleus and mitochondria/plastids. Although all RNase P enzymes catalyze the same reaction, the different architectures found in Eukarya range from ribonucleoprotein (RNP) enzymes with a catalytic RNA and up to 10 protein subunits to single-subunit protein-only RNase P (PRORP) enzymes. Here, analysis of the phylogenetic distribution of RNP and PRORP enzymes in Eukarya revealed 1) a wealth of novel P RNAs in previously unexplored phylogenetic branches and 2) that PRORP enzymes are more widespread than previously appreciated, found in four of the five eukaryal supergroups, in the nuclei and/or organelles. Intriguingly, the occurrence of RNP RNase P and PRORP seems mutually exclusive in genetic compartments of modern Eukarya. Our comparative analysis provides a global picture of the evolution and diversification of RNase P throughout Eukarya.Entities:
Keywords: PRORP; RNase P; eukaryal evolution; ribonucleoproteins; tRNA biogenesis
Mesh:
Substances:
Year: 2015 PMID: 26341299 DOI: 10.1093/molbev/msv187
Source DB: PubMed Journal: Mol Biol Evol ISSN: 0737-4038 Impact factor: 16.240