Structural features important for the RNA chaperone activity of zinc finger-containing glycine-rich RNA-binding proteins from wheat (Triticum avestivum) and rice (Oryza sativa)

Domain-swapping and deletion analysis established that the overall folding of RZs governed by the N-terminal RRM domain and the C-terminal glycine-rich region, as well as the size of the disordered C-terminal glycine-rich region, are crucial for RNA chaperone activity of RZs.