G- quadruplexes catalyze protein folding by reshaping the energetic landscape

成果类型:
Article
署名作者:
Huang, Zijue; Ghosh, Kingshuk; Stull, Frederick; Horowitz, Scott
署名单位:
University of Denver; University of Denver; University of Denver; Western Michigan University
刊物名称:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN/ISSBN:
0027-11294
DOI:
10.1073/pnas.2414045122
发表日期:
2025-02-03
关键词:
arc-repressor explorer
摘要:
Many proteins have slow folding times in vitro that are physiologically untenable. To combat this challenge, ATP- dependent chaperonins are thought to possess the unique ability to catalyze protein folding. Performing quantitative model selection using protein folding and unfolding data, we here show that short nucleic acids containing G- quadruplex (G4) structure can also catalyze protein folding. Performing the experiments as a function of temperature demonstrates that the G4 reshapes the underlying driving forces of protein folding. As short nucleic acids can catalyze protein folding without the input of ATP, the ability of the cell to fold proteins is far higher than previously anticipated.