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Mutagenesis and Analysis of Genetic Mutations in the GC-rich KISS1 Receptor Sequence Identified in Humans with Reproductive Disorders

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Structure-informed mutagenesis identifies a conserved region critical for mouse insulin receptor 5'UTR IRES function.

William B Dahl, Tammy C T Lan, Silvia Rouskin

Biorxiv : the Preprint Server for Biology

|November 22, 2024

Summary

Cells use internal ribosome entry sites (IRES) for translation during stress. Researchers mapped the insulin receptor 5' untranslated region (Insr 5'UTR) structure, identifying a key region for cap-independent translation.

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Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

Cells repress cap-dependent translation during stress.
Internal ribosome entry sites (IRES) enable translation of key transcripts under stress.
The RNA secondary structures of cellular IRESes are largely unknown.

Purpose of the Study:

To probe the secondary structure of the insulin receptor 5' untranslated region (Insr 5'UTR) IRES in cells.
To identify structural elements critical for Insr IRES function.
To design a minimal IRES element with high cap-independent translation activity.

Main Methods:

Dimethyl sulfate mutational profiling by sequencing (DMS-MaPseq) was used to probe RNA secondary structure in vitro and in cells.
A mutation strategy was employed, guided by a structural model of the Insr 5'UTR.
Viral IRESes (HCV, EMCV) were used as controls.

Main Results:

Viral IRES structures in cells were consistent with known in vitro structures.
Significant linearization of viral IRESes occurred near the translation start codon in cells.
A conserved segment of the Insr 5'UTR, distal to the start codon, was identified as critical for IRES activity.

Conclusions:

A structural model of the Insr 5'UTR was generated using DMS-MaPseq data.
A minimal Insr IRES element with full activity was designed.
This work elucidates cellular IRES structure and function, aiding stress response research.