Details

Autor(en) / Beteiligte

• Litberg, Theodore J.
• Sannapureddi, Rajesh Kumar Reddy
• Huang, Zijue
• Son, Ahyun
• Sathyamoorthy, Bharathwaj
• Horowitz, Scott

Titel

Why are G-quadruplexes good at preventing protein aggregation?

Ist Teil von

• RNA biology, 2023-12, Vol.20 (1), p.495-509

Ort / Verlag

United States: Taylor & Francis

Erscheinungsjahr

2023

Link zum Volltext

Quelle

Taylor & Francis Journals Auto-Holdings Collection

Beschreibungen/Notizen

• 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.