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Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks
Here, we investigate the function of fission yeast Fun30/Smarcad1 family of SNF2 ATPase-dependent chromatin remodeling enzymes in DNA damage repair. There are three Fun30 homologues in fission yeast, Fft1, Fft2, and Fft3. We find that only Fft3 has a function in DNA repair and it is needed for singl...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Life Science Alliance LLC
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6771652/ https://www.ncbi.nlm.nih.gov/pubmed/31575705 http://dx.doi.org/10.26508/lsa.201900433 |
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author | Ait-Saada, Anissia Khorosjutina, Olga Chen, Jiang Kramarz, Karol Maksimov, Vladimir Svensson, J Peter Lambert, Sarah Ekwall, Karl |
author_facet | Ait-Saada, Anissia Khorosjutina, Olga Chen, Jiang Kramarz, Karol Maksimov, Vladimir Svensson, J Peter Lambert, Sarah Ekwall, Karl |
author_sort | Ait-Saada, Anissia |
collection | PubMed |
description | Here, we investigate the function of fission yeast Fun30/Smarcad1 family of SNF2 ATPase-dependent chromatin remodeling enzymes in DNA damage repair. There are three Fun30 homologues in fission yeast, Fft1, Fft2, and Fft3. We find that only Fft3 has a function in DNA repair and it is needed for single-strand annealing of an induced double-strand break. Furthermore, we use an inducible replication fork barrier system to show that Fft3 has two distinct roles at blocked DNA replication forks. First, Fft3 is needed for the resection of nascent strands, and second, it is required to restart the blocked forks. The latter function is independent of its ATPase activity. |
format | Online Article Text |
id | pubmed-6771652 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Life Science Alliance LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-67716522019-10-02 Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks Ait-Saada, Anissia Khorosjutina, Olga Chen, Jiang Kramarz, Karol Maksimov, Vladimir Svensson, J Peter Lambert, Sarah Ekwall, Karl Life Sci Alliance Research Articles Here, we investigate the function of fission yeast Fun30/Smarcad1 family of SNF2 ATPase-dependent chromatin remodeling enzymes in DNA damage repair. There are three Fun30 homologues in fission yeast, Fft1, Fft2, and Fft3. We find that only Fft3 has a function in DNA repair and it is needed for single-strand annealing of an induced double-strand break. Furthermore, we use an inducible replication fork barrier system to show that Fft3 has two distinct roles at blocked DNA replication forks. First, Fft3 is needed for the resection of nascent strands, and second, it is required to restart the blocked forks. The latter function is independent of its ATPase activity. Life Science Alliance LLC 2019-10-01 /pmc/articles/PMC6771652/ /pubmed/31575705 http://dx.doi.org/10.26508/lsa.201900433 Text en © 2019 Ait-Saada et al. https://creativecommons.org/licenses/by/4.0/This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Articles Ait-Saada, Anissia Khorosjutina, Olga Chen, Jiang Kramarz, Karol Maksimov, Vladimir Svensson, J Peter Lambert, Sarah Ekwall, Karl Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks |
title | Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks |
title_full | Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks |
title_fullStr | Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks |
title_full_unstemmed | Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks |
title_short | Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks |
title_sort | chromatin remodeler fft3 plays a dual role at blocked dna replication forks |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6771652/ https://www.ncbi.nlm.nih.gov/pubmed/31575705 http://dx.doi.org/10.26508/lsa.201900433 |
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