Solution structure of RNase P RNA

Alexei V. Kazantsev, Robert P. Rambo, Sina Karimpour, John Santalucia, John A. Tainer, Norman R. Pace

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

The ribonucleoprotein enzyme ribonuclease P (RNase P) processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme: The RNA component catalyzes tRNA maturation in vitro without proteins. Remarkable features of RNase P include multiple turnovers in vivo and ability to process diverse substrates. Structures of the bacterial RNase P, including full-length RNAs and a ternary complex with substrate, have been determined by X-ray crystallography. However, crystal structures of free RNA are significantly different from the ternary complex, and the solution structure of the RNA is unknown. Here, we report solution structures of three phylogenetically distinct bacterial RNase P RNAs from Escherichia coli, Agrobacterium tumefaciens, and Bacillus stearothermophilus, determined using small angle X-ray scattering (SAXS) and selective 2′-hydroxyl acylation analyzed by primer extension (SHAPE) analysis. A combination of homology modeling, normal mode analysis, and molecular dynamics was used to refine the structural models against the empirical data of these RNAs in solution under the high ionic strength required for catalytic activity.

Original languageEnglish (US)
Pages (from-to)1159-1171
Number of pages13
JournalRNA
Volume17
Issue number6
DOIs
StatePublished - Jun 2011
Externally publishedYes

Keywords

  • Normal mode analysis
  • RNase P
  • Ribozyme
  • SAXS
  • Solution structure

ASJC Scopus subject areas

  • Molecular Biology

Fingerprint

Dive into the research topics of 'Solution structure of RNase P RNA'. Together they form a unique fingerprint.

Cite this