Life without RNase P

@article{Randau2008LifeWR,
  title={Life without RNase P},
  author={Lennart Randau and Imke Schr{\"o}der and Dieter S{\"o}ll},
  journal={Nature},
  year={2008},
  volume={453},
  pages={120-123}
}
The universality of ribonuclease P (RNase P), the ribonucleoprotein essential for transfer RNA (tRNA) 5′ maturation, is challenged in the archaeon Nanoarchaeum equitans. Neither extensive computational analysis of the genome nor biochemical tests in cell extracts revealed the existence of this enzyme. Here we show that the conserved placement of its tRNA gene promoters allows the synthesis of leaderless tRNAs, whose presence was verified by the observation of 5′ triphosphorylated mature tRNA… 
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TLDR
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TLDR
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Increased protein content correlated with evolution from bacteria to eukaryotes has further enhanced substrate potential enabling the enzyme to function in a complex cellular environment.
Generation of pre-tRNAs from polycistronic operons is the essential function of RNase P in Escherichia coli
TLDR
It is shown here for the first time that the processing of RNase P-dependent polycistronic tRNA operons to release pre-tRNAs is the essential function of the enzyme, since the majority of 5′-immature tRNAs can be aminoacylated unless their 5″-extensions ≥8 nt.
Insights into RNase P RNA structure and function by a retro-evolution approach
Ribonuclease P (RNase P) is a ribonucleoprotein enzyme that generates the mature 50 ends of tRNAs. Ubiquitous across all three kingdoms of life, the composition and functional contributions of the
Of P and Z: Mitochondrial tRNA processing enzymes☆
TLDR
The diversity of RNase P enzymes is contrasted by the uniformity of mitochondrial RNases Z, which are responsible for 3′-end processing.
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References

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TLDR
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TLDR
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