Of proteins and RNA: The RNase P/MRP family

Research output: Contribution to journalReview article

127 Citations (Scopus)

Abstract

Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse. RNA components of eukaryotic RNases P tend to be less complex than their bacterial counterparts, a simplification that is accompanied by a dramatic reduction of their catalytic ability in the absence of protein. The size and complexity of the protein moieties increase dramatically from bacterial to archaeal to eukaryotic enzymes, apparently reflecting the delegation of some structural functions from RNA to proteins and, perhaps, in response to the increased complexity of the cellular environment in the more evolutionarily advanced organisms; the reasons for the increased dependence on proteins are not clear. We review current information on RNase P and the closely related universal eukaryotic enzyme RNase MRP, focusing on their functions and structural organization.

Original languageEnglish (US)
Pages (from-to)1725-1747
Number of pages23
JournalRNA
Volume16
Issue number9
DOIs
StatePublished - Jan 1 2010

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Ribonuclease P
RNA
Proteins
Enzymes
Ribonucleoproteins
mitochondrial RNA-processing endoribonuclease

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

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abstract = "Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse. RNA components of eukaryotic RNases P tend to be less complex than their bacterial counterparts, a simplification that is accompanied by a dramatic reduction of their catalytic ability in the absence of protein. The size and complexity of the protein moieties increase dramatically from bacterial to archaeal to eukaryotic enzymes, apparently reflecting the delegation of some structural functions from RNA to proteins and, perhaps, in response to the increased complexity of the cellular environment in the more evolutionarily advanced organisms; the reasons for the increased dependence on proteins are not clear. We review current information on RNase P and the closely related universal eukaryotic enzyme RNase MRP, focusing on their functions and structural organization.",
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Of proteins and RNA : The RNase P/MRP family. / Esakova, Olga A.; Krasilnikov, Andrey S.

In: RNA, Vol. 16, No. 9, 01.01.2010, p. 1725-1747.

Research output: Contribution to journalReview article

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