Chemical shift assignments of N-terminal dsRNA binding domains dsRBD1 and dsRBD2 of Arabidopsis thaliana DRB5.

Abstract

Double-stranded RNA (dsRNA) binding proteins (dsRBPs) are among the key players that act along with other components involved in the RNA interference (RNAi) pathway for mediating gene silencing. Additionally, members of the dsRBP family of proteins play divergent roles in the broader array of biological processes. In Arabidopsis thaliana, dsRNA binding protein 5 (DRB5), along with DRB2 and DRB3, serves in recognition of viral RNA invasion and co-localizes with viral replication complexes. However, the functional role of DRB5 in such complexes is yet to be explored. DRB5 is a multidomain protein containing two tandem dsRNA binding domains (dsRBDs) at its N-terminus. Our current study presents the near-complete backbone and sidechain assignment of the dsRBD1 and dsRBD2 of DRB5 using solution NMR. The study will further contribute to determining the solution structure of dsRBDs and open new avenues to investigate the functional role of DRB5 in gene silencing pathways.