Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.

ABSTRACT: Posttranslational modifications can critically affect conformational changes of amyloid-forming proteins. Ubiquitination of the microtubule-associated tau protein, an intrinsically disordered biomolecule, has been proposed to influence the formation of filamentous deposits in neurodegenerative conditions. Given the reported link between aggregation propensity and intrinsic structural preferences (e.g., transient extended structural motifs or tertiary contacts) in disordered proteins, we sought to explore the conformational landscape of ubiquitinated tau. Exploiting selective conjugation reactions, we produced single- and double-monoubiquitinated protein samples. Next, we examined the ubiquitinated species from different standpoints using NMR spectroscopy, small-angle X-ray scattering exper

SUBMITTER: Viola G 

PROVIDER: S-EPMC12012461 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature