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Related Experiment Video

Updated: Jun 5, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

Substrate recognition by ribonucleoprotein ribonuclease MRP.

Olga Esakova¹, Anna Perederina, Chao Quan

¹Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.

RNA (New York, N.Y.)

|December 22, 2010

Summary

Ribonuclease (RNase) MRP, crucial for eukaryotic cell survival, was studied to understand its substrate recognition. Researchers identified specific sequence requirements near the cleavage site, revealing insights into its function.

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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

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Last Updated: Jun 5, 2026

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Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing (RIPiT-Seq)

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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Published on: September 29, 2012

Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Ribonucleoprotein complex ribonuclease (RNase) MRP is vital for eukaryotic cell survival.
RNase MRP is similar to RNase P but targets different RNA substrates like pre-rRNA and mRNA.

Purpose of the Study:

To identify specific substrate sequences recognized by Saccharomyces cerevisiae RNase MRP.
To elucidate the sequence requirements for RNase MRP cleavage activity.

Main Methods:

In vitro selection from a random RNA sequence pool.
Analysis of cleavage products to determine substrate specificity.

Main Results:

RNase MRP effectively cleaves single-stranded RNA.
Cleavage is sensitive to sequences near the cut site, specifically requiring a cytosine at the +4 position.

Conclusions:

RNase MRP exhibits distinct substrate recognition properties compared to RNase P.
These findings provide structural insights into the differential substrate binding of RNase P and RNase MRP.