Why are G-quadruplexes good at preventing protein aggregation?
Why are G-quadruplexes good at preventing protein aggregation?
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DOI:
10.1080/15476286.2023.2228572
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发表时间:
2023-01
期刊:
影响因子:
4.1
通讯作者:
Horowitz, Scott
中科院分区:
文献类型:
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作者:
Litberg, Theodore J.;Sannapureddi, Rajesh Kumar Reddy;Huang, Zijue;Son, Ahyun;Sathyamoorthy, Bharathwaj;Horowitz, Scott
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.
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DOI:
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发表时间:
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