Structural basis of nucleic acid recognition by the N-terminal cold shock domain of the plant glycine-rich protein AtGRP2.

ABSTRACT: AtGRP2 is a glycine-rich, RNA-binding protein that plays pivotal roles in abiotic stress response and flowering time regulation in Arabidopsis thaliana. AtGRP2 consists of an N-terminal cold shock domain (CSD) and two C-terminal CCHC-type zinc knuckles interspersed with glycine-rich regions. Here, we investigated the structure, dynamics, and nucleic acid-binding properties of AtGRP2-CSD. The 2D [¹H,¹⁵N] heteronuclear single quantum coherence spectrum of AtGRP2-CSD_1-79 revealed the presence of a partially folded intermediate in equilibrium with the folded state. The addition of 11 residues at the C terminus stabilized the folded conformation. The three-dimensional structure of AtGRP2-CSD_1-90 unveiled a β-barrel composed of five antiparallel β-stra

SUBMITTER: Pougy KC 

PROVIDER: S-EPMC11602973 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature