Substrate recognition by ribonucleoprotein ribonuclease MRP

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18 Scopus citations

Abstract

The ribonucleoprotein complex ribonuclease (RNase) MRP is a site-specific endoribonuclease essential for the survival of the eukaryotic cell. RNase MRP closely resembles RNase P (a universal endoribonuclease responsible for the maturation of the 5′ ends of tRNA) but recognizes distinct substrates including pre-rRNA and mRNA. Here we report the results of an in vitro selection of Saccharomyces cerevisiae RNase MRP substrates starting from a pool of random sequences. The results indicate that RNase MRP cleaves single-stranded RNA and is sensitive to sequences in the immediate vicinity of the cleavage site requiring a cytosine at the position +4 relative to the cleavage site. Structural implications of the differences in substrate recognition by RNases P and MRP are discussed.

Original languageEnglish (US)
Pages (from-to)356-364
Number of pages9
JournalRNA
Volume17
Issue number2
DOIs
StatePublished - Feb 2011

All Science Journal Classification (ASJC) codes

  • Molecular Biology

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