Effect of RNA sequence context and stereochemistry on G-quadruplex-RHAU53 interaction

Biochem Biophys Res Commun. 2020 Dec 17;533(4):1135-1141. doi: 10.1016/j.bbrc.2020.09.045. Epub 2020 Oct 9.


RNA G-quadruplex (rG4) structure and its association with rG4-binding proteins/peptides are important for its function. However, there is very limited study that investigates what factors are involved in rG4 that drive the rG4-protein/peptide interaction. Here we study and uncover the effect of RNA sequence context and stereochemistry on G-quadruplex-peptide interaction. Using rG4-binding RHAU53 peptide as an example, we report that the number of G-quartet, thermostability, overhanging nucleotides, and RNA base chirality have an impact on rG4-RHAU53 binding. Notably, our data also demonstrate that RHAU53 preferentially binds to 5' G-quartet over 3' G-quartet, and showcase that RHAU53 interacts with unnatural L-rG4 for the first time. Our findings reported here offer unique insights to the potential development of targeting tools that recognize rG4 structure and rG4-binding peptide/protein.

Keywords: G-quadruplex structure; RHAU53; RNA sequence context; RNA stereochemistry; RNA-Peptide interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs / genetics
  • Circular Dichroism
  • G-Quadruplexes*
  • Models, Molecular
  • Peptides / chemistry*
  • Peptides / genetics*
  • RNA / chemistry*
  • RNA / genetics*
  • Spectrophotometry, Ultraviolet
  • Thermodynamics


  • Peptides
  • RNA