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Updated: May 20, 2026

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

Using SecM arrest sequence as a tool to isolate ribosome bound polypeptides.

Sujata S Jha¹, Anton A Komar

¹Center for Gene Regulation in Health and Disease, Department of Biological, Geological and Environmental Sciences, Cleveland State University, USA.

Journal of Visualized Experiments : Jove

|July 4, 2012

Summary

This summary is machine-generated.

Understanding co-translational protein folding requires isolating ribosome-nascent chain complexes (RNCs). The SecM stalling sequence enables production of RNCs with specific nascent chain lengths for structural analysis.

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Area of Science:

Molecular Biology
Biochemistry
Structural Biology

Background:

Protein folding is a co-translational process, but the exact folding pathway remains unclear.
Isolating ribosome-nascent chain complexes (RNCs) of specific lengths is crucial for studying co-translational folding intermediates.
The SecM protein contains a 17-amino acid sequence that induces translational stalling.

Purpose of the Study:

To describe a method for isolating RNCs with predetermined nascent chain lengths.
To enable structural analysis of co-translational folding intermediates.
To isolate bovine Gamma-B Crystallin RNCs fused to the SecM stalling sequence.

Main Methods:

Utilizing the SecM stalling sequence fused to a target protein (bovine Gamma-B Crystallin).
Generating RNCs in an in vitro translation system.
Isolating RNCs using sucrose gradient centrifugation.

Main Results:

The SecM stalling sequence successfully arrested polypeptide chain elongation.
Stable RNCs carrying bovine Gamma-B Crystallin nascent chains of predetermined sizes were generated.
Isolated RNCs are suitable for structural and functional analysis of co-translational folding intermediates.

Conclusions:

The SecM stalling sequence is an effective tool for producing RNCs for co-translational folding studies.
This method facilitates the investigation of nascent chain structure and folding pathways.
The described technique advances our understanding of co-translational protein folding mechanisms.