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Related Experiment Video

Updated: Mar 20, 2026

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

Published on: February 18, 2022

A novel role for poly(C) binding proteins in programmed ribosomal frameshifting.

Sawsan Napthine¹, Emmely E Treffers², Susanne Bell¹

¹Department of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK.

Nucleic Acids Research

|June 4, 2016

Summary

This study reveals a novel viral mechanism where a protein complex, including a cellular poly(C) binding protein (PCBP), activates programmed ribosomal frameshifting (PRF) in viruses. This interaction highlights a new virus-host interaction pathway.

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Eukaryotic Polyribosome Profile Analysis

Published on: June 15, 2010

Area of Science:

Molecular Biology
Virology
Genetics

Background:

Programmed ribosomal frameshifting (PRF) regulates gene expression in viruses and cellular genes.
PRF is typically induced by mRNA secondary structures that affect ribosome fidelity at slippery sequences.

Purpose of the Study:

To investigate the mechanism of nsp2 programmed ribosomal frameshifting (PRF) in porcine reproductive and respiratory syndrome virus (PRRSV).
To identify the trans-acting protein factors involved in nsp2 PRF activation.

Main Methods:

In vitro translation assays to study ribosomal frameshifting.
Electrophoretic mobility shift assays (EMSAs) to analyze protein-RNA interactions.

Main Results:

A protein complex comprising viral nsp1β and cellular poly(C) binding protein (PCBP) was identified.
This PCBP/nsp1β complex binds to a C-rich region downstream of the PRRSV nsp2 slippery sequence.
The complex was shown to stimulate PRF, mimicking structured mRNA stimulators.

Conclusions:

This is the first demonstration of a cellular trans-acting protein's role in viral PRF.
The findings expand the known functions of poly(C) binding proteins.
A new class of virus-host interactions involving PCBP and viral proteins is proposed.