Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 117, Issue 42, Pages 26206-26217Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2000761117
Keywords
SSB; liquid-liquid phase separation; DNA repair; phase transition; membraneless organelle
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Funding
- Human Frontier Science Program [RGY0072/2010]
- Momentum Program of the Hungarian Academy of Sciences [LP2011-006/2011]
- ELTE (Eotvos Lorand University) [KMOP-4.2.1/B-10-2011-0002]
- NKFIH (National Research, Development and Innovation Office) [K-116072, NKFIH K123989, NKFIH ERC_HU 117680, NKFIH FK-128133, VEKOP-2.3.3-15-2016-00007]
- Premium Postdoctoral Program of the Hungarian Academy of Sciences [PREMIUM-2017-17, PREMIUM-2017-48]
- New National Excellence Program of the Ministry for Innovation and Technology [UNKP-19-3, UNKP-19-2]
- Hungarian Ministry for Innovation and Technology
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Bacterial single-stranded (ss)DNA-binding proteins (SSB) are essential for the replication and maintenance of the genome. SSBs share a conserved ssDNA-binding domain, a less conserved intrinsically disordered linker (IDL), and a highly conserved C-terminal peptide (CTP) motif that mediates a wide array of protein-protein interactions with DNA-metabolizing proteins. Here we show that the Escherichia coli SSB protein forms liquid-liquid phase-separated condensates in cellular-like conditions through multifaceted interactions involving all structural regions of the protein. SSB, ssDNA, and SSB-interacting molecules are highly concentrated within the condensates, whereas phase separation is overall regulated by the stoichiometry of SSB and ssDNA. Together with recent results on subcellular SSB localization patterns, our results point to a conserved mechanism by which bacterial cells store a pool of SSB and SSB-interacting proteins. Dynamic phase separation enables rapid mobilization of this protein pool to protect exposed ssDNA and repair genomic loci affected by DNA damage.
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