Structural Studies of Pif1 Helicases from Thermophilic Bacteria - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Microorganisms Année : 2023

Structural Studies of Pif1 Helicases from Thermophilic Bacteria

Résumé

Pif1 proteins are DNA helicases belonging to Superfamily 1, with 5 to 3 directionality. They are conserved from bacteria to human and have been shown to be particularly important in eukaryotes for replication and nuclear and mitochondrial genome stability. However, Pif1 functions in bacteria are less known. While most Pif1 from mesophilic bacteria consist of the helicase core with limited N-terminal and C-terminal extensions, some Pif1 from thermophilic bacteria exhibit a C-terminal WYL domain. We solved the crystal structures of Pif1 helicase cores from thermophilic bacteria Deferribacter desulfuricans and Sulfurihydrogenibium sp. in apo and nucleotide bound form. We show that the N-terminal part is important for ligand binding. The full-length Pif1 helicase was predicted based on the Alphafold algorithm and the nucleic acid binding on the Pif1 helicase core and the WYL domain was modelled based on known crystallographic structures. The model predicts that amino acids in the domains 1A, WYL, and linker between the Helicase core and WYL are important for nucleic acid binding. Therefore, the N-terminal and C-terminal extensions may be necessary to strengthen the binding of nucleic acid on these Pif1 helicases. This may be an adaptation to thermophilic conditions.
Fichier principal
Vignette du fichier
microorganisms-11-00479-v2.pdf (4.8 Mo) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte

Dates et versions

hal-04019847 , version 1 (08-03-2023)

Identifiants

Citer

Stéphane Réty, Yingzi Zhang, Wentong Fu, Shan Wang, Wei-Fei Chen, et al.. Structural Studies of Pif1 Helicases from Thermophilic Bacteria. Microorganisms, 2023, 11, ⟨10.3390/microorganisms11020479⟩. ⟨hal-04019847⟩
14 Consultations
15 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More