Cargando…
TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase
DNA topoisomerases are essential enzymes involved in all the DNA processes and among them, type IA topoisomerases emerged as a key actor in the maintenance of genome stability. The hyperthermophilic archaeon, Sulfolobus solfataricus, contains three topoisomerases IA including one classical named Top...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5778498/ https://www.ncbi.nlm.nih.gov/pubmed/29253195 http://dx.doi.org/10.1093/nar/gkx1247 |
_version_ | 1783294364522381312 |
---|---|
author | Bizard, Anna H Yang, Xi Débat, Hélène Fogg, Jonathan M Zechiedrich, Lynn Strick, Terence R Garnier, Florence Nadal, Marc |
author_facet | Bizard, Anna H Yang, Xi Débat, Hélène Fogg, Jonathan M Zechiedrich, Lynn Strick, Terence R Garnier, Florence Nadal, Marc |
author_sort | Bizard, Anna H |
collection | PubMed |
description | DNA topoisomerases are essential enzymes involved in all the DNA processes and among them, type IA topoisomerases emerged as a key actor in the maintenance of genome stability. The hyperthermophilic archaeon, Sulfolobus solfataricus, contains three topoisomerases IA including one classical named TopA. SsoTopA is very efficient at unlinking DNA catenanes, grouping SsoTopA into the topoisomerase III family. SsoTopA is active over a wide range of temperatures and at temperatures of up to 85°C it produces highly unwound DNA. At higher temperatures, SsoTopA unlinks the two DNA strands. Thus depending on the temperature, SsoTopA is able to either prevent or favor DNA melting. While canonical topoisomerases III require a single-stranded DNA region or a nick in one of the circles to decatenate them, we show for the first time that a type I topoisomerase, SsoTopA, is able to efficiently unlink covalently closed catenanes, with no additional partners. By using single molecule experiments we demonstrate that SsoTopA requires the presence of a short single-stranded DNA region to be efficient. The unexpected decatenation property of SsoTopA probably comes from its high ability to capture this unwound region. This points out a possible role of TopA in S. solfataricus as a decatenase in Sulfolobus. |
format | Online Article Text |
id | pubmed-5778498 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-57784982018-01-30 TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase Bizard, Anna H Yang, Xi Débat, Hélène Fogg, Jonathan M Zechiedrich, Lynn Strick, Terence R Garnier, Florence Nadal, Marc Nucleic Acids Res Nucleic Acid Enzymes DNA topoisomerases are essential enzymes involved in all the DNA processes and among them, type IA topoisomerases emerged as a key actor in the maintenance of genome stability. The hyperthermophilic archaeon, Sulfolobus solfataricus, contains three topoisomerases IA including one classical named TopA. SsoTopA is very efficient at unlinking DNA catenanes, grouping SsoTopA into the topoisomerase III family. SsoTopA is active over a wide range of temperatures and at temperatures of up to 85°C it produces highly unwound DNA. At higher temperatures, SsoTopA unlinks the two DNA strands. Thus depending on the temperature, SsoTopA is able to either prevent or favor DNA melting. While canonical topoisomerases III require a single-stranded DNA region or a nick in one of the circles to decatenate them, we show for the first time that a type I topoisomerase, SsoTopA, is able to efficiently unlink covalently closed catenanes, with no additional partners. By using single molecule experiments we demonstrate that SsoTopA requires the presence of a short single-stranded DNA region to be efficient. The unexpected decatenation property of SsoTopA probably comes from its high ability to capture this unwound region. This points out a possible role of TopA in S. solfataricus as a decatenase in Sulfolobus. Oxford University Press 2018-01-25 2017-12-14 /pmc/articles/PMC5778498/ /pubmed/29253195 http://dx.doi.org/10.1093/nar/gkx1247 Text en © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Nucleic Acid Enzymes Bizard, Anna H Yang, Xi Débat, Hélène Fogg, Jonathan M Zechiedrich, Lynn Strick, Terence R Garnier, Florence Nadal, Marc TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase |
title | TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase |
title_full | TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase |
title_fullStr | TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase |
title_full_unstemmed | TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase |
title_short | TopA, the Sulfolobus solfataricus topoisomerase III, is a decatenase |
title_sort | topa, the sulfolobus solfataricus topoisomerase iii, is a decatenase |
topic | Nucleic Acid Enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5778498/ https://www.ncbi.nlm.nih.gov/pubmed/29253195 http://dx.doi.org/10.1093/nar/gkx1247 |
work_keys_str_mv | AT bizardannah topathesulfolobussolfataricustopoisomeraseiiiisadecatenase AT yangxi topathesulfolobussolfataricustopoisomeraseiiiisadecatenase AT debathelene topathesulfolobussolfataricustopoisomeraseiiiisadecatenase AT foggjonathanm topathesulfolobussolfataricustopoisomeraseiiiisadecatenase AT zechiedrichlynn topathesulfolobussolfataricustopoisomeraseiiiisadecatenase AT strickterencer topathesulfolobussolfataricustopoisomeraseiiiisadecatenase AT garnierflorence topathesulfolobussolfataricustopoisomeraseiiiisadecatenase AT nadalmarc topathesulfolobussolfataricustopoisomeraseiiiisadecatenase |