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Nucleic Acids Res. 2013 Aug;41(14):7084-91. doi: 10.1093/nar/gkt432. Epub 2013 May 21.

Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.

Author information

1
Department of Biochemistry and Molecular Biology and Center for RNA Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.

Abstract

Ribonuclease (RNase) MRP is a ubiquitous and essential site-specific eukaryotic endoribonuclease involved in the metabolism of a wide range of RNA molecules. RNase MRP is a ribonucleoprotein with a large catalytic RNA moiety that is closely related to the RNA component of RNase P, and multiple proteins, most of which are shared with RNase P. Here, we report the results of an ultraviolet-cross-linking analysis of interactions between a photoreactive RNase MRP substrate and the Saccharomyces cerevisiae RNase MRP holoenzyme. The results show that the substrate interacts with phylogenetically conserved RNA elements universally found in all enzymes of the RNase P/MRP family, as well as with a phylogenetically conserved RNA region that is unique to RNase MRP, and demonstrate that four RNase MRP protein components, all shared with RNase P, interact with the substrate. Implications for the structural organization of RNase MRP and the roles of its components are discussed.

PMID:
23700311
PMCID:
PMC3737539
DOI:
10.1093/nar/gkt432
[Indexed for MEDLINE]
Free PMC Article

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