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Defining the Intrinsically Disordered C-Terminal Domain of SSB Reveals DNA-Mediated Compaction.

Matthew Green¹, Louise Hatter², Emre Brookes³

¹Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, United Kingdom.

Journal of Molecular Biology

|December 29, 2015

Summary

Bacterial single-stranded DNA binding protein (SSB) C-terminal arms collapse upon DNA binding, contrary to previous models. This collapse mechanism traps DNA and recruits partner proteins for essential cellular functions.

Keywords:

Bacillus subtilis SANS SASSIE SAXS intrinsic disorder

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Area of Science:

Molecular Biology
Structural Biology
Biochemistry

Background:

Bacterial single-stranded DNA binding protein (SSB) is essential for DNA replication and repair.
SSB has a structured core that binds DNA and disordered C-terminal domains for protein interactions.

Purpose of the Study:

To elucidate the structural mechanism of SSB's C-terminal domains during DNA binding.
To challenge the prevailing model of C-terminal arm expansion upon ssDNA binding.

Main Methods:

Combined small-angle X-ray and neutron scattering (SAXS/SANS).
Coarse-grained computational modeling.
Structural analysis of SSB-ssDNA interactions.

Main Results:

Contrary to the established model, SSB's intrinsically disordered C-terminal arms collapse around the core upon ssDNA binding.
The C-terminal domain collapse is a dynamic process that enhances upon DNA interaction.
This collapse mechanism facilitates ssDNA binding and recruitment of partner proteins.

Conclusions:

The study reveals a novel mechanism for SSB function, involving C-terminal domain collapse rather than expansion.
This finding redefines the understanding of how SSB interacts with DNA and partner proteins.
The collapsed C-terminal domains play a crucial role in stabilizing DNA-protein complexes and mediating functional interactions.