G‐Quadruplexes act as sequence‐dependent protein chaperones. (18th September 2020)

• Record Type: Journal Article
• Authors: Begeman, Adam; Son, Ahyun; Litberg, Theodore J; Wroblewski, Tadeusz H; Gehring, Thane; Huizar Cabral, Veronica; Bourne, Jennifer; Xuan, Zhenyu; Horowitz, Scott
• Is Part Of: EMBO reports. Volume 21:Number 10(2020)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2020-09-18
• Subjects: nucleic acids -- protein aggregation -- protein folding -- proteostasis -- RNA; Molecular biology -- Periodicals; Molecular Biology -- Periodicals; Molecular biology; Periodicals; 572.8
• DOI: 10.15252/embr.201949735
• Languages: English
• ISSNs: 1469-221X

Abstract

Abstract: Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent protein aggregation more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaperone activity of nucleic acids. Evaluating over 500 nucleic acid sequences' effects on protein aggregation, we show that the holdase chaperone effect of nucleic acids is sequence‐dependent. G‐Quadruplexes prevent protein aggregation via quadruplex:protein oligomerization. They also increase the folded protein level of a biosensor in E. coli . These observations contextualize recent reports of quadruplexes playing important roles in aggregation‐related diseases, such as fragile X and amyotrophic lateral sclerosis (ALS), and provide evidence that nucleic acids have the ability to modulate the folding environment of E. coli . Synopsis: Examining nucleic acids for the sequence dependence of their chaperone activity finds quadruplexes have potent roles in protein oligomerization and aggregation prevention. Chaperone nucleic acid activity is sequence dependent. Quadruplexes modulate protein oligomerization. Chaperone nucleic acid activity can occur in E. coli . Abstract : Examining nucleic acids for the sequence dependence of their chaperone activity finds quadruplexes have potent roles in protein oligomerization and aggregation prevention.