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Article

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

1
Laboratoire de Microbiologie et Génétique Moléculaires, UMR5100, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, Université Paul Sabatier, F-31062 Toulouse, France
2
Laboratory of Applied Biotechnology (LBA3B), Azm Center for Research in Biotechnology and Its Application, EDST, Lebanese University, Tripoli 1300, Lebanon
3
Ifremer, Univ Brest, CNRS, UMR 6197 Laboratoire de Microbiologie des Environnements Extrêmes, F-29280 Plouzané, France
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Laboratoire de Biologie Moléculaire, Cellulaire et du Développement, UMR5077, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, Université Paul Sabatier, F-31062 Toulouse, France
*
Authors to whom correspondence should be addressed.
Co-first authors.
Academic Editor: Hannu Myllykallio
Biomolecules 2021, 11(7), 950; https://doi.org/10.3390/biom11070950
Received: 23 December 2020 / Revised: 18 June 2021 / Accepted: 23 June 2021 / Published: 26 June 2021
(This article belongs to the Collection Archaea: Diversity, Metabolism and Molecular Biology)
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. View Full-Text
Keywords: SF2 helicases; aLhr2 helicases; archaea; RNA metabolism; DNA repair; Thermococcales SF2 helicases; aLhr2 helicases; archaea; RNA metabolism; DNA repair; Thermococcales
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MDPI and ACS Style

Hajj, M.; Langendijk-Genevaux, P.; Batista, M.; Quentin, Y.; Laurent, S.; Capeyrou, R.; Abdel-Razzak, Z.; Flament, D.; Chamieh, H.; Fichant, G.; Clouet-d’Orval, B.; Bouvier, M. Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase. Biomolecules 2021, 11, 950. https://doi.org/10.3390/biom11070950

AMA Style

Hajj M, Langendijk-Genevaux P, Batista M, Quentin Y, Laurent S, Capeyrou R, Abdel-Razzak Z, Flament D, Chamieh H, Fichant G, Clouet-d’Orval B, Bouvier M. Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase. Biomolecules. 2021; 11(7):950. https://doi.org/10.3390/biom11070950

Chicago/Turabian Style

Hajj, Mirna, Petra Langendijk-Genevaux, Manon Batista, Yves Quentin, Sébastien Laurent, Régine Capeyrou, Ziad Abdel-Razzak, Didier Flament, Hala Chamieh, Gwennaele Fichant, Béatrice Clouet-d’Orval, and Marie Bouvier. 2021. "Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase" Biomolecules 11, no. 7: 950. https://doi.org/10.3390/biom11070950

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