Switch-like compaction of poly(ADP-ribose) upon cation binding.

ABSTRACT: Poly(ADP-ribose) (PAR) is a homopolymer of adenosine diphosphate ribose that is added to proteins as a posttranslational modification to regulate numerous cellular processes. PAR also serves as a scaffold for protein binding in macromolecular complexes, including biomolecular condensates. It remains unclear how PAR achieves specific molecular recognition. Here, we use single-molecule fluorescence resonance energy transfer (smFRET) to evaluate PAR flexibility under different cation conditions. We demonstrate that, compared to RNA and DNA, PAR has a longer persistence length and undergoes a sharper transition from extended to compact states in physiologically relevant concentrations of various cations (Na⁺, Mg²⁺, Ca²⁺, and spermine⁴⁺). We show that

SUBMITTER: Badiee M 

PROVIDER: S-EPMC10175808 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature