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Updated: Jul 13, 2026

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
Published on: September 28, 2017
The R3H domain stabilizes poly(A)-specific ribonuclease by stabilizing the RRM domain
Wei-Feng Liu1, Ao Zhang, Guang-Jun He
1State Key Laboratory of Biomembrane and Membrane Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
Abstract:
Poly(A)-specific ribonuclease (PARN), a key enzyme involved in eukaryotic mRNA decay, contains one catalytic domain and two RNA-binding domains. Here we found that at least one RNA-binding domain is required for the substrate binding, but not for the catalysis of PARN. The removal of the R3H domain led to a dramatic decrease in PARN stability and a change in the aggregation kinetic regime, while only minor effects were observed for the removal of the RRM domain or both RNA-binding domains. Thus the R3H domain might stabilize PARN by acting as a protector or intermolecular chaperone of the RRM domain.
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