NMR-based conformational analysis of DNA G-quadruplex guides mapping essential structure-function relationship in protein chaperoning.

ABSTRACT: G-quadruplexes (G4s) are increasingly recognized to chaperone proteins, warranting studies of structure-function relationships. In this study, we apply solution NMR methods to determine the topology and base-level resolution structure of a G-rich DNA sequence with protein chaperoning activity (referred to as Seq576) without chemical shift assignments. Seq576 samples two conformations, in the slow exchange timescale, arising from a G-register shift. Using the structural insights of Seq576, we then perform structure-function studies via mutation and chaperone assays to investigate the G4 properties essential for chaperoning protein aggregation and folding. These studies highlight the possibility of using a construct design to perform in-depth nucleic acid structural biology investigat

SUBMITTER: Negi D 

PROVIDER: S-EPMC12766885 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature