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Updated: Jul 12, 2026

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

Published on: February 9, 2009

A simplified and high-yield purification method for recombinant RNase R.

Wataru Horikawa^1,2,3,4, Daniel L Kiss^1,2,3,5,6,7

¹Center for RNA Therapeutics, Houston, TX, United States.

Micropublication Biology

|July 10, 2026

Summary

This summary is machine-generated.

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Researchers developed a cost-effective method to produce high-quality RNase R, an enzyme crucial for circular RNA (circRNA) research. This accessible purification technique ensures complete linear RNA digestion, making circRNA analysis and production more attainable.

Area of Science:

Biochemistry
Molecular Biology
RNA Biology

Background:

Ribonuclease R (RNase R) is a 3'→5' exoribonuclease essential for RNA processing.
RNase R is critical for the production and analysis of circular RNAs (circRNAs).
The high cost of commercial RNase R limits its widespread use in research and therapeutic development.

Purpose of the Study:

To develop an accessible and cost-effective method for purifying recombinant RNase R.
To demonstrate that the purified enzyme exhibits performance comparable to commercial RNase R.

Main Methods:

Recombinant RNase R was expressed in E. coli.
A single-step purification using Ni NTA chromatography was performed on an entry-level FPLC system.
The enzyme's activity was assessed by its ability to degrade linear RNAs while preserving circRNAs.

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Last Updated: Jul 12, 2026

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

Published on: February 9, 2009

Rapid Production of Recombinant Human SLFN14 Ribonuclease and Stoichiometric Analysis by Mass Photometry

Rapid Production of Recombinant Human SLFN14 Ribonuclease and Stoichiometric Analysis by Mass Photometry

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Main Results:

High-quality recombinant RNase R was successfully purified using a cost-effective, single-step chromatography method.
The purified enzyme demonstrated efficient digestion of linear RNAs.
The enzyme effectively maintained the integrity of circRNAs, matching the performance of commercial RNase R.

Conclusions:

A practical and economical method for producing functional RNase R has been established.
This accessible purification strategy can lower the barrier for utilizing RNase R in circRNA research and development.
The recombinant RNase R produced is a viable alternative to expensive commercial preparations.