The protein cofactor allows the sequence of an RNase P ribozyme to diversify by maintaining the catalytically active structure of the enzyme

Joseph J. Kim, Ahmed F. Kilani, Xiaoyan Zhan, Sidney Altman, Fenyong Liu

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

To study the effect proteins have on the catalysis and evolution of RNA enzymes, we simulated evolution of RNase P catalytic M1 RNA in vitro, in the presence and absence of its C5 protein cofactor. In the presence of C5, functional M1 sequence variants (not catalytically active in the absence of C5) were selected in addition to those identical to M1. C5 maintains the catalytically active structure of the variants and allows for an enhanced spectrum of M1 molecules to function in the context of a ribonucleoprotein (RNP) complex. The generation of an RNP enzyme, requiring both RNA and protein components, from a catalytically active RNA molecule has implications for how modern RNP complexes evolved from ancestral RNAs.

Original languageEnglish (US)
Pages (from-to)613-623
Number of pages11
JournalRNA
Volume3
Issue number6
StatePublished - Jun 1 1997
Externally publishedYes

Keywords

  • C5 protein
  • RNA catalysis
  • RNase P
  • catalytic RNA
  • in vitro evolution
  • tRNA

ASJC Scopus subject areas

  • Molecular Biology

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