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Updated: Jun 26, 2025

An Assay for Quantifying Protein-RNA Binding in Bacteria

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The mutation R107Q alters mtSSB ssDNA compaction ability and binding dynamics.

Martial Martucci¹, Amandine Moretton¹, Aleix Tarrés-Solé²

¹Université Clermont Auvergne, CNRS, Laboratoire de Physique de Clermont, F-63000 Clermont-Ferrand, France.

Nucleic Acids Research

|May 14, 2024

Summary

This summary is machine-generated.

The R107Q mutation impairs mitochondrial single-stranded DNA-binding protein (mtSSB) function, reducing its ability to bind and compact single-stranded DNA (ssDNA). This molecular defect is linked to mitochondrial optic atrophy and retinal dystrophy.

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Area of Science:

Mitochondrial biology
Molecular genetics
Biochemistry

Background:

Mitochondrial single-stranded DNA-binding protein (mtSSB) is crucial for mitochondrial DNA (mtDNA) replication.
mtSSB variants are implicated in autosomal dominant mitochondrial optic atrophy and retinal dystrophy.

Purpose of the Study:

To investigate the molecular mechanisms underlying the severe R107Q mtSSB variant.
To elucidate the functional consequences of the R107Q mutation on mtSSB's interaction with single-stranded DNA (ssDNA).

Main Methods:

In vitro analysis of mtSSB R107Q oligomeric state.
Single-molecule approaches to assess ssDNA binding and compaction.
Real-time competition assays for ssDNA binding.
Molecular modeling of ssDNA interaction with mtSSB.

Main Results:

The mtSSBR107Q mutant forms stable tetramers in vitro.
mtSSBR107Q exhibits reduced ssDNA compaction and increased ssDNA dissociation compared to wild-type (WT) mtSSB.
WT mtSSB demonstrated a significant advantage over mtSSBR107Q in ssDNA binding competition.
Molecular modeling suggests the R107Q mutation disrupts electrostatic interactions, reducing ssDNA binding sites.

Conclusions:

The R107Q mutation severely impairs mtSSB's ssDNA-binding and compaction capabilities.
These functional deficits are likely due to weakened ssDNA wrapping efficiency and altered protein-ssDNA interactions.
The findings provide molecular insights into the pathogenesis of mtSSB-associated mitochondrial diseases.