Single molecule microscopy reveals key physical features of repair foci in living cells

In response to double strand breaks (DSB), repair proteins accumulate at damaged sites, forming membrane-less sub-compartments or foci. Here we explored the physical nature of these foci, using single molecule microscopy in living cells. Rad52, the functional homolog of BRCA2 in yeast, accumulates a...

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Published in:	eLife Vol. 10
Main Authors:	Miné-Hattab, Judith, Heltberg, Mathias, Villemeur, Marie, Guedj, Chloé, Mora, Thierry, Walczak, Aleksandra M, Dahan, Maxime, Taddei, Angela
Format:	Journal Article
Language:	English
Published:	England eLife Sciences Publications Ltd 05.02.2021 eLife Sciences Publication eLife Sciences Publications, Ltd
Subjects:	BRCA2 protein Cell cycle Chromatin DNA Damage DNA repair Life Sciences liquid-liquid phase separation Microscopy nuclear sub-compartments Physics of Living Systems Population Proteins Rad52 DNA Repair and Recombination Protein - chemistry Rad52 protein Replication Protein A - chemistry Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae Proteins - chemistry Single Molecule Imaging single molecule microscopy single particle tracking Yeast nuclear sub-compartments liquid-liquid phase separation single particle tracking single molecule microscopy DNA repair physics of living systems S. cerevisiae
ISSN:	2050-084X, 2050-084X
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Abstract	In response to double strand breaks (DSB), repair proteins accumulate at damaged sites, forming membrane-less sub-compartments or foci. Here we explored the physical nature of these foci, using single molecule microscopy in living cells. Rad52, the functional homolog of BRCA2 in yeast, accumulates at DSB sites and diffuses ~6 times faster within repair foci than the focus itself, exhibiting confined motion. The Rad52 confinement radius coincides with the focus size: foci resulting from 2 DSBs are twice larger in volume that the ones induced by a unique DSB and the Rad52 confinement radius scales accordingly. In contrast, molecules of the single strand binding protein Rfa1 follow anomalous diffusion similar to the focus itself or damaged chromatin. We conclude that while most Rfa1 molecules are bound to the ssDNA, Rad52 molecules are free to explore the entire focus reflecting the existence of a liquid droplet around damaged DNA.
AbstractList	In response to double strand breaks (DSB), repair proteins accumulate at damaged sites, forming membrane-less sub-compartments or foci. Here we explored the physical nature of these foci, using single molecule microscopy in living cells. Rad52, the functional homolog of BRCA2 in yeast, accumulates at DSB sites and diffuses ~6 times faster within repair foci than the focus itself, exhibiting confined motion. The Rad52 confinement radius coincides with the focus size: foci resulting from 2 DSBs are twice larger in volume that the ones induced by a unique DSB and the Rad52 confinement radius scales accordingly. In contrast, molecules of the single strand binding protein Rfa1 follow anomalous diffusion similar to the focus itself or damaged chromatin. We conclude that while most Rfa1 molecules are bound to the ssDNA, Rad52 molecules are free to explore the entire focus reflecting the existence of a liquid droplet around damaged DNA.In response to double strand breaks (DSB), repair proteins accumulate at damaged sites, forming membrane-less sub-compartments or foci. Here we explored the physical nature of these foci, using single molecule microscopy in living cells. Rad52, the functional homolog of BRCA2 in yeast, accumulates at DSB sites and diffuses ~6 times faster within repair foci than the focus itself, exhibiting confined motion. The Rad52 confinement radius coincides with the focus size: foci resulting from 2 DSBs are twice larger in volume that the ones induced by a unique DSB and the Rad52 confinement radius scales accordingly. In contrast, molecules of the single strand binding protein Rfa1 follow anomalous diffusion similar to the focus itself or damaged chromatin. We conclude that while most Rfa1 molecules are bound to the ssDNA, Rad52 molecules are free to explore the entire focus reflecting the existence of a liquid droplet around damaged DNA. In response to double strand breaks (DSB), repair proteins accumulate at damaged sites, forming membrane-less sub-compartments or foci. Here we explored the physical nature of these foci, using single molecule microscopy in living cells. Rad52, the functional homolog of BRCA2 in yeast, accumulates at DSB sites and diffuses ~6 times faster within repair foci than the focus itself, exhibiting confined motion. The Rad52 confinement radius coincides with the focus size: foci resulting from 2 DSBs are twice larger in volume that the ones induced by a unique DSB and the Rad52 confinement radius scales accordingly. In contrast, molecules of the single strand binding protein Rfa1 follow anomalous diffusion similar to the focus itself or damaged chromatin. We conclude that while most Rfa1 molecules are bound to the ssDNA, Rad52 molecules are free to explore the entire focus reflecting the existence of a liquid droplet around damaged DNA.
Author	Taddei, Angela Villemeur, Marie Walczak, Aleksandra M Dahan, Maxime Heltberg, Mathias Guedj, Chloé Mora, Thierry Miné-Hattab, Judith
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Keywords	nuclear sub-compartments liquid-liquid phase separation single particle tracking single molecule microscopy DNA repair physics of living systems S. cerevisiae
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Snippet	In response to double strand breaks (DSB), repair proteins accumulate at damaged sites, forming membrane-less sub-compartments or foci. Here we explored the...
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SubjectTerms	BRCA2 protein Cell cycle Chromatin DNA Damage DNA repair Life Sciences liquid-liquid phase separation Microscopy nuclear sub-compartments Physics of Living Systems Population Proteins Rad52 DNA Repair and Recombination Protein - chemistry Rad52 protein Replication Protein A - chemistry Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae Proteins - chemistry Single Molecule Imaging single molecule microscopy single particle tracking Yeast
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Title	Single molecule microscopy reveals key physical features of repair foci in living cells
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