Why are G-quadruplexes good at preventing protein aggregation?
RNA Biol
; 20(1): 495-509, 2023 01.
Article
in En
| MEDLINE
| ID: mdl-37493593
ABSTRACT
Maintaining a healthy protein folding environment is essential for cellular function. Recently, we found that nucleic acids, G-quadruplexes in particular, are potent chaperones for preventing protein aggregation. With the aid of structure-function and NMR analyses of two G-quadruplex forming sequences, PARP-I and LTR-III, we uncovered several contributing factors that affect G-quadruplexes in preventing protein aggregation. Notably, three factors emerged as vital in determining holdase activity of G-quadruplexes their structural topology, G-quadruplex accessibility and dynamics, and oligomerization state. These factors together appear to largely dictate whether a G-quadruplex is able to prevent partially misfolded proteins from aggregating. Understanding the physical traits that govern the ability of G-quadruplexes to modulate protein aggregation will help elucidate their possible roles in neurodegenerative disease.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Neurodegenerative Diseases
/
G-Quadruplexes
Limits:
Humans
Language:
En
Journal:
RNA Biol
Journal subject:
BIOLOGIA MOLECULAR
Year:
2023
Type:
Article
Affiliation country:
United States