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Structural characterisation of the Chaetomium thermophilum Chl1 helicase

Chl1 is a member of the XPD family of 5’-3’ DNA helicases, which perform a variety of roles in genome maintenance and transmission. They possess a variety of unique structural features, including the presence of a highly variable, partially-ordered insertion in the helicase domain 1. Chl1 has been s...

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Autores principales: Hodáková, Zuzana, Nans, Andrea, Kunzelmann, Simone, Mehmood, Shahid, Taylor, Ian, Uhlmann, Frank, Cherepanov, Peter, Singleton, Martin R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8109800/
https://www.ncbi.nlm.nih.gov/pubmed/33970942
http://dx.doi.org/10.1371/journal.pone.0251261
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author Hodáková, Zuzana
Nans, Andrea
Kunzelmann, Simone
Mehmood, Shahid
Taylor, Ian
Uhlmann, Frank
Cherepanov, Peter
Singleton, Martin R.
author_facet Hodáková, Zuzana
Nans, Andrea
Kunzelmann, Simone
Mehmood, Shahid
Taylor, Ian
Uhlmann, Frank
Cherepanov, Peter
Singleton, Martin R.
author_sort Hodáková, Zuzana
collection PubMed
description Chl1 is a member of the XPD family of 5’-3’ DNA helicases, which perform a variety of roles in genome maintenance and transmission. They possess a variety of unique structural features, including the presence of a highly variable, partially-ordered insertion in the helicase domain 1. Chl1 has been shown to be required for chromosome segregation in yeast due to its role in the formation of persistent chromosome cohesion during S-phase. Here we present structural and biochemical data to show that Chl1 has the same overall domain organisation as other members of the XPD family, but with some conformational alterations. We also present data suggesting the insert domain in Chl1 regulates its DNA binding.
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spelling pubmed-81098002021-05-21 Structural characterisation of the Chaetomium thermophilum Chl1 helicase Hodáková, Zuzana Nans, Andrea Kunzelmann, Simone Mehmood, Shahid Taylor, Ian Uhlmann, Frank Cherepanov, Peter Singleton, Martin R. PLoS One Research Article Chl1 is a member of the XPD family of 5’-3’ DNA helicases, which perform a variety of roles in genome maintenance and transmission. They possess a variety of unique structural features, including the presence of a highly variable, partially-ordered insertion in the helicase domain 1. Chl1 has been shown to be required for chromosome segregation in yeast due to its role in the formation of persistent chromosome cohesion during S-phase. Here we present structural and biochemical data to show that Chl1 has the same overall domain organisation as other members of the XPD family, but with some conformational alterations. We also present data suggesting the insert domain in Chl1 regulates its DNA binding. Public Library of Science 2021-05-10 /pmc/articles/PMC8109800/ /pubmed/33970942 http://dx.doi.org/10.1371/journal.pone.0251261 Text en © 2021 Hodáková et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Hodáková, Zuzana
Nans, Andrea
Kunzelmann, Simone
Mehmood, Shahid
Taylor, Ian
Uhlmann, Frank
Cherepanov, Peter
Singleton, Martin R.
Structural characterisation of the Chaetomium thermophilum Chl1 helicase
title Structural characterisation of the Chaetomium thermophilum Chl1 helicase
title_full Structural characterisation of the Chaetomium thermophilum Chl1 helicase
title_fullStr Structural characterisation of the Chaetomium thermophilum Chl1 helicase
title_full_unstemmed Structural characterisation of the Chaetomium thermophilum Chl1 helicase
title_short Structural characterisation of the Chaetomium thermophilum Chl1 helicase
title_sort structural characterisation of the chaetomium thermophilum chl1 helicase
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8109800/
https://www.ncbi.nlm.nih.gov/pubmed/33970942
http://dx.doi.org/10.1371/journal.pone.0251261
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