Cargando…
hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress
The maintenance of genome stability is an essential cellular process to prevent the development of diseases including cancer. hSSB1 (NABP2/ OBFC2A) is a critical component of the DNA damage response where it participates in the repair of double-strand DNA breaks and in base excision repair of oxidiz...
Autores principales: | , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4897654/ https://www.ncbi.nlm.nih.gov/pubmed/27273218 http://dx.doi.org/10.1038/srep27446 |
_version_ | 1782436207504916480 |
---|---|
author | Paquet, Nicolas Adams, Mark N. Ashton, Nicholas W. Touma, Christine Gamsjaeger, Roland Cubeddu, Liza Leong, Vincent Beard, Sam Bolderson, Emma Botting, Catherine H. O’Byrne, Kenneth J. Richard, Derek J. |
author_facet | Paquet, Nicolas Adams, Mark N. Ashton, Nicholas W. Touma, Christine Gamsjaeger, Roland Cubeddu, Liza Leong, Vincent Beard, Sam Bolderson, Emma Botting, Catherine H. O’Byrne, Kenneth J. Richard, Derek J. |
author_sort | Paquet, Nicolas |
collection | PubMed |
description | The maintenance of genome stability is an essential cellular process to prevent the development of diseases including cancer. hSSB1 (NABP2/ OBFC2A) is a critical component of the DNA damage response where it participates in the repair of double-strand DNA breaks and in base excision repair of oxidized guanine residues (8-oxoguanine) by aiding the localization of the human 8-oxoguanine glycosylase (hOGG1) to damaged DNA. Here we demonstrate that following oxidative stress, hSSB1 is stabilized as an oligomer which is required for hSSB1 to function in the removal of 8-oxoguanine. Monomeric hSSB1 shows a decreased affinity for oxidized DNA resulting in a cellular 8-oxoguanine-repair defect and in the absence of ATM signaling initiation. While hSSB1 oligomerization is important for the removal of 8-oxoguanine from the genome, it is not required for the repair of double-strand DNA-breaks by homologous recombination. These findings demonstrate a novel hSSB1 regulatory mechanism for the repair of damaged DNA. |
format | Online Article Text |
id | pubmed-4897654 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48976542016-06-10 hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress Paquet, Nicolas Adams, Mark N. Ashton, Nicholas W. Touma, Christine Gamsjaeger, Roland Cubeddu, Liza Leong, Vincent Beard, Sam Bolderson, Emma Botting, Catherine H. O’Byrne, Kenneth J. Richard, Derek J. Sci Rep Article The maintenance of genome stability is an essential cellular process to prevent the development of diseases including cancer. hSSB1 (NABP2/ OBFC2A) is a critical component of the DNA damage response where it participates in the repair of double-strand DNA breaks and in base excision repair of oxidized guanine residues (8-oxoguanine) by aiding the localization of the human 8-oxoguanine glycosylase (hOGG1) to damaged DNA. Here we demonstrate that following oxidative stress, hSSB1 is stabilized as an oligomer which is required for hSSB1 to function in the removal of 8-oxoguanine. Monomeric hSSB1 shows a decreased affinity for oxidized DNA resulting in a cellular 8-oxoguanine-repair defect and in the absence of ATM signaling initiation. While hSSB1 oligomerization is important for the removal of 8-oxoguanine from the genome, it is not required for the repair of double-strand DNA-breaks by homologous recombination. These findings demonstrate a novel hSSB1 regulatory mechanism for the repair of damaged DNA. Nature Publishing Group 2016-06-08 /pmc/articles/PMC4897654/ /pubmed/27273218 http://dx.doi.org/10.1038/srep27446 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Paquet, Nicolas Adams, Mark N. Ashton, Nicholas W. Touma, Christine Gamsjaeger, Roland Cubeddu, Liza Leong, Vincent Beard, Sam Bolderson, Emma Botting, Catherine H. O’Byrne, Kenneth J. Richard, Derek J. hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress |
title | hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress |
title_full | hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress |
title_fullStr | hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress |
title_full_unstemmed | hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress |
title_short | hSSB1 (NABP2/OBFC2B) is regulated by oxidative stress |
title_sort | hssb1 (nabp2/obfc2b) is regulated by oxidative stress |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4897654/ https://www.ncbi.nlm.nih.gov/pubmed/27273218 http://dx.doi.org/10.1038/srep27446 |
work_keys_str_mv | AT paquetnicolas hssb1nabp2obfc2bisregulatedbyoxidativestress AT adamsmarkn hssb1nabp2obfc2bisregulatedbyoxidativestress AT ashtonnicholasw hssb1nabp2obfc2bisregulatedbyoxidativestress AT toumachristine hssb1nabp2obfc2bisregulatedbyoxidativestress AT gamsjaegerroland hssb1nabp2obfc2bisregulatedbyoxidativestress AT cubedduliza hssb1nabp2obfc2bisregulatedbyoxidativestress AT leongvincent hssb1nabp2obfc2bisregulatedbyoxidativestress AT beardsam hssb1nabp2obfc2bisregulatedbyoxidativestress AT boldersonemma hssb1nabp2obfc2bisregulatedbyoxidativestress AT bottingcatherineh hssb1nabp2obfc2bisregulatedbyoxidativestress AT obyrnekennethj hssb1nabp2obfc2bisregulatedbyoxidativestress AT richardderekj hssb1nabp2obfc2bisregulatedbyoxidativestress |