Cargando…
Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication
Accurate completion of replication relies on the ability of cells to activate error-free recombination-mediated DNA damage bypass at sites of perturbed replication. However, as anti-recombinase activities are also recruited to replication forks, how recombination-mediated damage bypass is enabled at...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4604347/ https://www.ncbi.nlm.nih.gov/pubmed/26443850 http://dx.doi.org/10.1101/gad.265629.115 |
_version_ | 1782395048511406080 |
---|---|
author | Urulangodi, Madhusoodanan Sebesta, Marek Menolfi, Demis Szakal, Barnabas Sollier, Julie Sisakova, Alexandra Krejci, Lumir Branzei, Dana |
author_facet | Urulangodi, Madhusoodanan Sebesta, Marek Menolfi, Demis Szakal, Barnabas Sollier, Julie Sisakova, Alexandra Krejci, Lumir Branzei, Dana |
author_sort | Urulangodi, Madhusoodanan |
collection | PubMed |
description | Accurate completion of replication relies on the ability of cells to activate error-free recombination-mediated DNA damage bypass at sites of perturbed replication. However, as anti-recombinase activities are also recruited to replication forks, how recombination-mediated damage bypass is enabled at replication stress sites remained puzzling. Here we uncovered that the conserved SUMO-like domain-containing Saccharomyces cerevisiae protein Esc2 facilitates recombination-mediated DNA damage tolerance by allowing optimal recruitment of the Rad51 recombinase specifically at sites of perturbed replication. Mechanistically, Esc2 binds stalled replication forks and counteracts the anti-recombinase Srs2 helicase via a two-faceted mechanism involving chromatin recruitment and turnover of Srs2. Importantly, point mutations in the SUMO-like domains of Esc2 that reduce its interaction with Srs2 cause suboptimal levels of Rad51 recruitment at damaged replication forks. In conclusion, our results reveal how recombination-mediated DNA damage tolerance is locally enabled at sites of replication stress and globally prevented at undamaged replicating chromosomes. |
format | Online Article Text |
id | pubmed-4604347 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-46043472015-10-19 Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication Urulangodi, Madhusoodanan Sebesta, Marek Menolfi, Demis Szakal, Barnabas Sollier, Julie Sisakova, Alexandra Krejci, Lumir Branzei, Dana Genes Dev Research Paper Accurate completion of replication relies on the ability of cells to activate error-free recombination-mediated DNA damage bypass at sites of perturbed replication. However, as anti-recombinase activities are also recruited to replication forks, how recombination-mediated damage bypass is enabled at replication stress sites remained puzzling. Here we uncovered that the conserved SUMO-like domain-containing Saccharomyces cerevisiae protein Esc2 facilitates recombination-mediated DNA damage tolerance by allowing optimal recruitment of the Rad51 recombinase specifically at sites of perturbed replication. Mechanistically, Esc2 binds stalled replication forks and counteracts the anti-recombinase Srs2 helicase via a two-faceted mechanism involving chromatin recruitment and turnover of Srs2. Importantly, point mutations in the SUMO-like domains of Esc2 that reduce its interaction with Srs2 cause suboptimal levels of Rad51 recruitment at damaged replication forks. In conclusion, our results reveal how recombination-mediated DNA damage tolerance is locally enabled at sites of replication stress and globally prevented at undamaged replicating chromosomes. Cold Spring Harbor Laboratory Press 2015-10-01 /pmc/articles/PMC4604347/ /pubmed/26443850 http://dx.doi.org/10.1101/gad.265629.115 Text en © 2015 Urulangodi et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by/4.0/ This article, published in Genes & Development, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Research Paper Urulangodi, Madhusoodanan Sebesta, Marek Menolfi, Demis Szakal, Barnabas Sollier, Julie Sisakova, Alexandra Krejci, Lumir Branzei, Dana Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication |
title | Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication |
title_full | Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication |
title_fullStr | Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication |
title_full_unstemmed | Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication |
title_short | Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication |
title_sort | local regulation of the srs2 helicase by the sumo-like domain protein esc2 promotes recombination at sites of stalled replication |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4604347/ https://www.ncbi.nlm.nih.gov/pubmed/26443850 http://dx.doi.org/10.1101/gad.265629.115 |
work_keys_str_mv | AT urulangodimadhusoodanan localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication AT sebestamarek localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication AT menolfidemis localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication AT szakalbarnabas localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication AT sollierjulie localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication AT sisakovaalexandra localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication AT krejcilumir localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication AT branzeidana localregulationofthesrs2helicasebythesumolikedomainproteinesc2promotesrecombinationatsitesofstalledreplication |