Bespoke RNA recognition by Pumilios

Biochem Soc Trans. 2015 Oct;43(5):801-6. doi: 10.1042/BST20150072.

Abstract

Pumilio is an RNA-binding protein originally identified in Drosophila, with a Puf domain made up of eight Puf repeats, three helix bundles arranged in a rainbow architecture, where each repeat recognizes a single base of the RNA-binding sequence. The eight-base recognition sequence can therefore be modified simply via mutation of the repeat that recognizes the base to be changed and this is understood in detail via high-resolution crystal structures. The binding mechanism is also altered in a variety of homologues from different species, with bases flipped out from the binding site to regenerate a consensus sequence. Thus Pumilios can be designed with bespoke RNA recognition sequences and can be fused to nucleases, split GFP, etc. as tools in vitro and in cells.

Keywords: Puf domain; Pumilio; hunchback; ribonucleic acid (RNA) recognition; ribonucleic acid (RNA)-binding protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Binding Sites
  • Humans
  • Hydrogen Bonding
  • Models, Molecular*
  • Mutation
  • Nucleic Acid Conformation
  • Protein Conformation
  • Protein Engineering
  • Protein Interaction Domains and Motifs
  • RNA / chemistry
  • RNA / metabolism*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*

Substances

  • PUM1 protein, human
  • PUM2 protein, human
  • RNA-Binding Proteins
  • RNA