title: Engineering RNA-binding proteins for biology.
abstract: RNA-binding proteins play essential roles in the regulation of gene expression. Many have modular structures and combine relatively few common domains in various arrangements to recognize RNA sequences and/or structures. Recent progress in engineering the specificity of the PUF class RNA-binding proteins has shown that RNA-binding domains may be combined with various effector or functional domains to regulate the metabolism of targeted RNAs. Designer RNA-binding proteins with tailored sequence specificity will provide valuable tools for biochemical research as well as potential therapeutic applications. In this review, we discuss the suitability of various RNA-binding domains for engineering RNA-binding specificity, based on the structural basis for their recognition. We also compare various protein engineering and design methods applied to RNA-binding proteins, and discuss future applications of these proteins.
authors.affiliation: Department of Biochemistry, University of Washington, Seattle, WA 98195-1700, USA. chenyu@u.washington.edu
authors.forename: Yu
authors.initials: Y
authors.lastname: Chen
authors.forename: Gabriele
authors.initials: G
authors.lastname: Varani
mesh_terms: D000818:Animals; D035843:Biomedical Research; D015195:Drug Design; D006801:Humans; D008958:Models, Molecular; D015202:Protein Engineering; D054730:Protein Interaction Domains and Motifs; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000627:therapeutic use; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism / Q000627:therapeutic use; D016335:Zinc Fingers
chemical_list: D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins
keywords: RNA recognition motif; RNA-binding domains; RNA-binding proteins; computational design; in vitro evolution; phage display; protein engineering; protein-RNA interactions; yeast three-hybrid system; zinc finger