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Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase

Helicase proteins are known to use the energy of ATP to unwind nucleic acids and to remodel protein-nucleic acid complexes. They are involved in almost every aspect of DNA and RNA metabolisms and participate in numerous repair mechanisms that maintain cellular integrity. The archaeal Lhr-type protei...

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Autores principales: Hajj, Mirna, Langendijk-Genevaux, Petra, Batista, Manon, Quentin, Yves, Laurent, Sébastien, Capeyrou, Régine, Abdel-Razzak, Ziad, Flament, Didier, Chamieh, Hala, Fichant, Gwennaele, Clouet-d’Orval, Béatrice, Bouvier, Marie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8301817/
https://www.ncbi.nlm.nih.gov/pubmed/34206878
http://dx.doi.org/10.3390/biom11070950
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author Hajj, Mirna
Langendijk-Genevaux, Petra
Batista, Manon
Quentin, Yves
Laurent, Sébastien
Capeyrou, Régine
Abdel-Razzak, Ziad
Flament, Didier
Chamieh, Hala
Fichant, Gwennaele
Clouet-d’Orval, Béatrice
Bouvier, Marie
author_facet Hajj, Mirna
Langendijk-Genevaux, Petra
Batista, Manon
Quentin, Yves
Laurent, Sébastien
Capeyrou, Régine
Abdel-Razzak, Ziad
Flament, Didier
Chamieh, Hala
Fichant, Gwennaele
Clouet-d’Orval, Béatrice
Bouvier, Marie
author_sort Hajj, Mirna
collection PubMed
description Helicase proteins are known to use the energy of ATP to unwind nucleic acids and to remodel protein-nucleic acid complexes. They are involved in almost every aspect of DNA and RNA metabolisms and participate in numerous repair mechanisms that maintain cellular integrity. The archaeal Lhr-type proteins are SF2 helicases that are mostly uncharacterized. They have been proposed to be DNA helicases that act in DNA recombination and repair processes in Sulfolobales and Methanothermobacter. In Thermococcales, a protein annotated as an Lhr2 protein was found in the network of proteins involved in RNA metabolism. To investigate this, we performed in-depth phylogenomic analyses to report the classification and taxonomic distribution of Lhr-type proteins in Archaea, and to better understand their relationship with bacterial Lhr. Furthermore, with the goal of envisioning the role(s) of aLhr2 in Thermococcales cells, we deciphered the enzymatic activities of aLhr2 from Thermococcus barophilus (Tbar). We showed that Tbar-aLhr2 is a DNA/RNA helicase with a significant annealing activity that is involved in processes dependent on DNA and RNA transactions.
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spelling pubmed-83018172021-07-24 Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase Hajj, Mirna Langendijk-Genevaux, Petra Batista, Manon Quentin, Yves Laurent, Sébastien Capeyrou, Régine Abdel-Razzak, Ziad Flament, Didier Chamieh, Hala Fichant, Gwennaele Clouet-d’Orval, Béatrice Bouvier, Marie Biomolecules Article Helicase proteins are known to use the energy of ATP to unwind nucleic acids and to remodel protein-nucleic acid complexes. They are involved in almost every aspect of DNA and RNA metabolisms and participate in numerous repair mechanisms that maintain cellular integrity. The archaeal Lhr-type proteins are SF2 helicases that are mostly uncharacterized. They have been proposed to be DNA helicases that act in DNA recombination and repair processes in Sulfolobales and Methanothermobacter. In Thermococcales, a protein annotated as an Lhr2 protein was found in the network of proteins involved in RNA metabolism. To investigate this, we performed in-depth phylogenomic analyses to report the classification and taxonomic distribution of Lhr-type proteins in Archaea, and to better understand their relationship with bacterial Lhr. Furthermore, with the goal of envisioning the role(s) of aLhr2 in Thermococcales cells, we deciphered the enzymatic activities of aLhr2 from Thermococcus barophilus (Tbar). We showed that Tbar-aLhr2 is a DNA/RNA helicase with a significant annealing activity that is involved in processes dependent on DNA and RNA transactions. MDPI 2021-06-26 /pmc/articles/PMC8301817/ /pubmed/34206878 http://dx.doi.org/10.3390/biom11070950 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hajj, Mirna
Langendijk-Genevaux, Petra
Batista, Manon
Quentin, Yves
Laurent, Sébastien
Capeyrou, Régine
Abdel-Razzak, Ziad
Flament, Didier
Chamieh, Hala
Fichant, Gwennaele
Clouet-d’Orval, Béatrice
Bouvier, Marie
Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase
title Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase
title_full Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase
title_fullStr Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase
title_full_unstemmed Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase
title_short Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase
title_sort phylogenetic diversity of lhr proteins and biochemical activities of the thermococcales alhr2 dna/rna helicase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8301817/
https://www.ncbi.nlm.nih.gov/pubmed/34206878
http://dx.doi.org/10.3390/biom11070950
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