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Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...

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DNA Tension Probes to Map the Transient Piconewton Receptor Forces by Immune Cells

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Published on: March 20, 2021

Measuring bridging forces in protein-DNA condensates.

Vikhyaat Ahlawat^1,2, Hashini Ekanayake Mudiyanselage¹, Divya Kota¹

¹Department of Chemistry, University of Illinois Chicago, Chicago, IL 60607.

Proceedings of the National Academy of Sciences of the United States of America

|January 13, 2026

Summary

This summary is machine-generated.

Protein-DNA condensates regulate gene expression. Researchers measured bridging forces, finding the DNA structure (single-stranded vs. double-stranded) and ratio tune condensate stability and behavior.

Keywords:

biomolecular condensates bridging forces optical tweezers single-molecule force spectroscopy

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Area of Science:

Biophysics
Molecular Biology
Genetics

Background:

Protein-DNA condensates are crucial for cellular processes like transcription and DNA repair.
The forces stabilizing these condensates play a key role in their function.

Purpose of the Study:

To quantitatively measure the intermolecular bridging forces within protein-DNA condensates.
To investigate how DNA structure (single-stranded vs. double-stranded) and ratio influence these forces and condensate properties.

Main Methods:

Utilized optical tweezers to precisely measure single-molecule bridging forces.
Analyzed force curves to understand condensate disassembly mechanisms.
Investigated the impact of varying single-stranded DNA (ssDNA) to double-stranded DNA (dsDNA) ratios on condensate behavior.

Main Results:

Single-stranded DNA (ssDNA) condensates showed sequential bridge rupture with forces of 11.3 ± 4.6 pN.
Double-stranded DNA (dsDNA) formed stable tangles withstanding ~60 pN forces.
Increased dsDNA content raised bridging forces to 34 ± 8 pN, while adding ssDNA reduced them to ~10 pN.
Protamine-dsDNA mixtures formed solid-like aggregates, transitioning to liquid droplets upon ssDNA addition.

Conclusions:

The ssDNA-to-dsDNA ratio is a critical determinant of bridging force magnitude in protein-DNA condensates.
This ratio can dynamically tune condensate properties, shifting them between liquid-like and solid-like states.
Understanding these forces provides insights into the regulation of gene expression and DNA-related processes.