The P3 domain of eukaryotic RNases P/MRP: Making a protein-rich RNA-based enzyme

Research output: Contribution to journalReview article

9 Citations (Scopus)

Abstract

Nuclear Ribonuclease (RNase) P is a universal essential RNA-based enzyme made of a catalytic RNA component and a protein part; eukaryotic RNase P is closely related to a universal eukaryotic ribonucleoprotein RNase MRP. The protein part of the eukaryotic RNases P/MRP is dramatically more complex than that in bacterial and archaeal RNases P. The increase in the complexity of the protein part in eukaryotic RNases P/MRP was accompanied by the appearance of a novel structural element in the RNA component: an essential and phylogenetically conserved helix-loop-helix P3 RNA domain. The crystal structure of the P3 RNA domain in a complex with protein components Pop6 and Pop7 has been recently solved. Here we discuss the most salient structural features of the P3 domain as well as its possible role in the evolutionary transition to the protein-rich eukaryotic RNases P/MRP.

Original languageEnglish (US)
Pages (from-to)534-539
Number of pages6
JournalRNA Biology
Volume7
Issue number5
DOIs
StatePublished - Jan 1 2010

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Ribonuclease P
RNA
Enzymes
Proteins
Catalytic RNA
Ribonucleoproteins

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

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The P3 domain of eukaryotic RNases P/MRP : Making a protein-rich RNA-based enzyme. / Perederina, Anna; Krasilnikov, Andrey S.

In: RNA Biology, Vol. 7, No. 5, 01.01.2010, p. 534-539.

Research output: Contribution to journalReview article

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