Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA

Nicholas J. Reiter, Amy Osterman, Alfredo Torres-Larios, Kerren K. Swinger, Tao Pan, Alfonso Mondragón*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

179 Scopus citations

Abstract

Ribonuclease (RNase) P is the universal ribozyme responsible for 5-2-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNA Phe. The 154-‰kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a mature tRNA. The structure shows that RNA-RNA recognition occurs through shape complementarity, specific intermolecular contacts and base-pairing interactions. Soaks with a pre-tRNA 5-2 leader sequence with and without metal help to identify the 5-2 substrate path and potential catalytic metal ions. The protein binds on top of a universally conserved structural module in P RNA and interacts with the leader, but not with the mature tRNA. The active site is composed of phosphate backbone moieties, a universally conserved uridine nucleobase, and at least two catalytically important metal ions. The active site structure and conserved RNase P-tRNA contacts suggest a universal mechanism of catalysis by RNase P.

Original languageEnglish (US)
Pages (from-to)784-791
Number of pages8
JournalNature
Volume468
Issue number7325
DOIs
StatePublished - Dec 9 2010

ASJC Scopus subject areas

  • General

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