Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA

Nicholas J. Reiter, Amy Osterman, Alfredo Torres-Larios, Kerren K. Swinger, Tao Pan and Alfonso Mondragón ()
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Nicholas J. Reiter: Northwestern University
Amy Osterman: Northwestern University
Alfredo Torres-Larios: Northwestern University
Kerren K. Swinger: Northwestern University
Tao Pan: University of Chicago
Alfonso Mondragón: Northwestern University

Nature, 2010, vol. 468, issue 7325, 784-789

Abstract: Abstract Ribonuclease (RNase) P is the universal ribozyme responsible for 5′-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNAPhe. 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′ leader sequence with and without metal help to identify the 5′ 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.

Date: 2010
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DOI: 10.1038/nature09516

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