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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 30 Dec 2024

Martínez-Carranza M, Vialle L, Madru C, Cordier F, Tekpinar AD, Haouz A, Legrand P, Le Meur RA, England P, Dulermo R, Guijarro JI, Henneke G, Sauguet L

Link to Pubmed [PMID] – 39738083

Link to DOI – 10.1038/s41467-024-55365-w

Nat Commun 2024 Dec; 15(1): 10926

Replication Protein A (RPA) plays a pivotal role in DNA replication by coating and protecting exposed single-stranded DNA, and acting as a molecular hub that recruits additional replication factors. We demonstrate that archaeal RPA hosts a winged-helix domain (WH) that interacts with two key actors of the replisome: the DNA primase (PriSL) and the replicative DNA polymerase (PolD). Using an integrative structural biology approach, combining nuclear magnetic resonance, X-ray crystallography and cryo-electron microscopy, we unveil how RPA interacts with PriSL and PolD through two distinct surfaces of the WH domain: an evolutionarily conserved interface and a novel binding site. Finally, RPA is shown to stimulate the activity of PriSL in a WH-dependent manner. This study provides a molecular understanding of the WH-mediated regulatory activity in central replication factors such as RPA, which regulate genome maintenance in Archaea and Eukaryotes.