Cargando…
Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor
Prolonged pausing of the transcription machinery may lead to the formation of three-stranded nucleic acid structures, called R-loops, typically resulting from the annealing of the nascent RNA with the template DNA. Unscheduled persistence of R-loops and RNA polymerases may interfere with transcripti...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10085699/ https://www.ncbi.nlm.nih.gov/pubmed/36864660 http://dx.doi.org/10.1093/nar/gkad092 |
_version_ | 1785021990705299456 |
---|---|
author | Hasanova, Zdenka Klapstova, Veronika Porrua, Odil Stefl, Richard Sebesta, Marek |
author_facet | Hasanova, Zdenka Klapstova, Veronika Porrua, Odil Stefl, Richard Sebesta, Marek |
author_sort | Hasanova, Zdenka |
collection | PubMed |
description | Prolonged pausing of the transcription machinery may lead to the formation of three-stranded nucleic acid structures, called R-loops, typically resulting from the annealing of the nascent RNA with the template DNA. Unscheduled persistence of R-loops and RNA polymerases may interfere with transcription itself and other essential processes such as DNA replication and repair. Senataxin (SETX) is a putative helicase, mutated in two neurodegenerative disorders, which has been implicated in the control of R-loop accumulation and in transcription termination. However, understanding the precise role of SETX in these processes has been precluded by the absence of a direct characterisation of SETX biochemical activities. Here, we purify and characterise the helicase domain of SETX in parallel with its yeast orthologue, Sen1. Importantly, we show that SETX is a bona fide helicase with the ability to resolve R-loops. Furthermore, SETX has retained the transcription termination activity of Sen1 but functions in a species-specific manner. Finally, subsequent characterisation of two SETX variants harbouring disease-associated mutations shed light into the effect of such mutations on SETX folding and biochemical properties. Altogether, these results broaden our understanding of SETX function in gene expression and the maintenance of genome integrity and provide clues to elucidate the molecular basis of SETX-associated neurodegenerative diseases. |
format | Online Article Text |
id | pubmed-10085699 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-100856992023-04-11 Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor Hasanova, Zdenka Klapstova, Veronika Porrua, Odil Stefl, Richard Sebesta, Marek Nucleic Acids Res Nucleic Acid Enzymes Prolonged pausing of the transcription machinery may lead to the formation of three-stranded nucleic acid structures, called R-loops, typically resulting from the annealing of the nascent RNA with the template DNA. Unscheduled persistence of R-loops and RNA polymerases may interfere with transcription itself and other essential processes such as DNA replication and repair. Senataxin (SETX) is a putative helicase, mutated in two neurodegenerative disorders, which has been implicated in the control of R-loop accumulation and in transcription termination. However, understanding the precise role of SETX in these processes has been precluded by the absence of a direct characterisation of SETX biochemical activities. Here, we purify and characterise the helicase domain of SETX in parallel with its yeast orthologue, Sen1. Importantly, we show that SETX is a bona fide helicase with the ability to resolve R-loops. Furthermore, SETX has retained the transcription termination activity of Sen1 but functions in a species-specific manner. Finally, subsequent characterisation of two SETX variants harbouring disease-associated mutations shed light into the effect of such mutations on SETX folding and biochemical properties. Altogether, these results broaden our understanding of SETX function in gene expression and the maintenance of genome integrity and provide clues to elucidate the molecular basis of SETX-associated neurodegenerative diseases. Oxford University Press 2023-03-02 /pmc/articles/PMC10085699/ /pubmed/36864660 http://dx.doi.org/10.1093/nar/gkad092 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://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 Hasanova, Zdenka Klapstova, Veronika Porrua, Odil Stefl, Richard Sebesta, Marek Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor |
title | Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor |
title_full | Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor |
title_fullStr | Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor |
title_full_unstemmed | Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor |
title_short | Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor |
title_sort | human senataxin is a bona fide r-loop resolving enzyme and transcription termination factor |
topic | Nucleic Acid Enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10085699/ https://www.ncbi.nlm.nih.gov/pubmed/36864660 http://dx.doi.org/10.1093/nar/gkad092 |
work_keys_str_mv | AT hasanovazdenka humansenataxinisabonafiderloopresolvingenzymeandtranscriptionterminationfactor AT klapstovaveronika humansenataxinisabonafiderloopresolvingenzymeandtranscriptionterminationfactor AT porruaodil humansenataxinisabonafiderloopresolvingenzymeandtranscriptionterminationfactor AT steflrichard humansenataxinisabonafiderloopresolvingenzymeandtranscriptionterminationfactor AT sebestamarek humansenataxinisabonafiderloopresolvingenzymeandtranscriptionterminationfactor |