Effect of RNA sequence context and stereochemistry on G-quadruplex-RHAU53 interaction
|Journal / Publication||Biochemical and Biophysical Research Communications|
|Online published||9 Oct 2020|
|Publication status||Published - 17 Dec 2020|
|Link to Scopus||https://www.scopus.com/record/display.uri?eid=2-s2.0-85092261197&origin=recordpage|
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.
- G-quadruplex structure, RHAU53, RNA sequence context, RNA stereochemistry, RNA-Peptide interaction
Biochemical and Biophysical Research Communications, Vol. 533, No. 4, 17.12.2020, p. 1135-1141.
Research output: Journal Publications and Reviews (RGC: 21, 22, 62) › 21_Publication in refereed journal › peer-review