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Biochem Biophys Res Commun. 2011 Oct 28;414(3):517-22. doi: 10.1016/j.bbrc.2011.09.098. Epub 2011 Sep 24.

Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3.

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  • 1Department of Biochemistry, University of Texas Health Science Center at San Antonio San Antonio, TX 78229-3900, USA.

Abstract

Ribonuclease P (RNase P) is a ubiquitous trans-acting ribozyme that processes the 5' leader sequence of precursor tRNA (pre-tRNA). The RNase P RNA (PhopRNA) of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 is central to the catalytic process and binds five proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) which contribute to the enzymatic activity of the holoenzyme. Despite significant progress in determining the crystal structure of the proteins, the structure of PhopRNA remains elusive. Comparative analysis of the RNase P RNA sequences and existing crystallographic structural information of the bacterial RNase P RNAs were combined to generate a phylogenetically supported three-dimensional (3-D) model of the PhopRNA. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. Moreover, the structure in solution was investigated by enzymatic probing and small-angle X-ray scattering (SAXS) analysis. The low resolution model derived from SAXS and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme.

Copyright © 2011 Elsevier Inc. All rights reserved.

PMID:
21968019
[PubMed - indexed for MEDLINE]
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