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Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2062-7. Epub 2007 Feb 6.

Eukaryotic RNase P RNA mediates cleavage in the absence of protein.

Author information

  • 1Department of Cell and Molecular Biology, Uppsala University, Box 596, Biomedical Centre, SE-751 24 Uppsala, Sweden.

Erratum in

  • Proc Natl Acad Sci U S A. 2009 May 12;106(19):8078.

Abstract

The universally conserved ribonucleoprotein RNase P is involved in the processing of tRNA precursor transcripts. RNase P consists of one RNA and, depending on its origin, a variable number of protein subunits. Catalytic activity of the RNA moiety so far has been demonstrated only for bacterial and some archaeal RNase P RNAs but not for their eukaryotic counterparts. Here, we show that RNase P RNAs from humans and the lower eukaryote Giardia lamblia mediate cleavage of four tRNA precursors and a model RNA hairpin loop substrate in the absence of protein. Compared with bacterial RNase P RNA, the rate of cleavage (k(obs)) was five to six orders of magnitude lower, whereas the affinity for the substrate (appK(d)) was reduced approximately 20- to 50-fold. We conclude that the RNA-based catalytic activity of RNase P has been preserved during evolution. This finding opens previously undescribed ways to study the role of the different proteins subunits of eukaryotic RNase P.

Comment in

  • Uniformity amid diversity in RNase P. [Proc Natl Acad Sci U S A. 2007]
PMID:
17284611
[PubMed - indexed for MEDLINE]
PMCID:
PMC1892975
Free PMC Article

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