Multiple RNA- and DNA-binding proteins exhibit direct transfer of polynucleotides with implications for target-site search.

ABSTRACT: We previously demonstrated that the polycomb repressive complex 2 chromatin-modifying enzyme can directly transfer between RNA and DNA without a free-enzyme intermediate state. Simulations suggested that such a direct transfer mechanism may be generally necessary for RNA to recruit proteins to chromatin, but the prevalence of direct transfer capability is unknown. Herein, we used fluorescence polarization assays and observed direct transfer for several well-characterized nucleic acid-binding proteins: three-prime repair exonuclease 1, heterogeneous nuclear ribonucleoprotein U, Fem-3-binding factor 2, and MS2 bacteriophage coat protein. For TREX1, the direct transfer mechanism was additionally observed in single-molecule assays, and the data suggest that direct transfer occurs through an un

SUBMITTER: Hemphill WO 

PROVIDER: S-EPMC10293810 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature