Na-Nv Liu

Article Dans Une Revue Nucleic Acids Research Année : 2024 Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition Origine : Fichiers éditeurs autorisés sur une archive ouverte hal-04472793 , version 1 (22-02-2024) Ben-Ge Xin, Ling-Yun Huang, Ling-Gang Yuan, Na-Nv Liu, Hai-Hong Li, et al.. Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition. Nucleic Acids Research, In press, ⟨10.1093/nar/gkae138⟩.

Inherently disordered N- and C-tails confer full helicase activities to the Dbp2 protein To probe the spatial conformation of N- and C-tails relative to the full-length Dbp2 in solution, SAXS assays were performed. Figure S6A is the experimental SAXS profile of Dbp2. The EOM ( ) analysis was carried out for Dbp2 by introducing flexibility in the N-and C-tails, and in the linker between the helicase core. An atomic model was finally obtained with χ 2of 1.62 (Fig. 5A).

Helicases play a critical role in processes such as replication or recombination by unwinding double-stranded DNA; mutations of these genes can therefore have devastating biological consequences. In humans, mutations in genes of three members of the RecQ family helicases (blm, wrn, and recq4) give rise to three strikingly distinctive clinical phenotypes: Bloom syndrome, Werner syndrome, and Rothmund-Thomson syndrome, respectively.