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

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review

4 Scopus Citations
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Original languageEnglish
Pages (from-to)1135-1141
Journal / PublicationBiochemical and Biophysical Research Communications
Issue number4
Online published9 Oct 2020
Publication statusPublished - 17 Dec 2020


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.

Research Area(s)

  • G-quadruplex structure, RHAU53, RNA sequence context, RNA stereochemistry, RNA-Peptide interaction