Crystal structures of Caenorhabditis elegans PUF-3 depict plasticity of RNA recognition that enables germline gene regulation.

ABSTRACT: Prototypical PUF proteins are known for modular, sequence-specific RNA recognition. A single PUF protein in Drosophila melanogaster Pumilio and two closely related proteins in mammals, PUM1 and PUM2, are representative. In contrast, Caenorhabditis elegans PUF proteins have evolved to include four subfamilies of single-stranded RNA-binding proteins that recognize distinct sequence elements. Here, we provide an in-depth structural and biochemical analysis of C. elegans PUF-3, a member of the subfamily lacking structural information. We determined crystal structures of PUF-3 in complex with RNAs representing three classes of binding elements. These structures and quantitative RNA-binding assays fine-tune the features of PUF-3 RNA recognition and demonstrate how PUF-3 binds to varied target RN

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC12774653 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature