@article{d55117305bee4f2eb72cd7c0a430d4a2,
title = "Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding",
abstract = "The Escherichia coli GroEL/ES chaperonin system facilitates protein folding in an ATP-driven manner. There are <100 obligate clients of this system in E. coli although GroEL can interact and assist the folding of a multitude of proteins in vitro. It has remained unclear, however, which features distinguish obligate clients from all the other proteins in an E. coli cell. To address this question, we established a system for selecting mutations in mouse dihydrofolate reductase (mDHFR), a GroEL interactor, that diminish its dependence on GroEL for folding. Strikingly, both synonymous and non-synonymous codon substitutions were found to reduce mDHFR's dependence on GroEL. The non-synonymous substitutions increase the rate of spontaneous folding whereas computational analysis indicates that the synonymous substitutions appear to affect translation rates at specific sites.",
keywords = "GroEL, chaperonins, codon usage, protein folding, random mutagenesis",
author = "Reingewertz, {Tali Haviv} and Miki Ben-Maimon and Zohar Zafrir and Tamir Tuller and Amnon Horovitz",
note = "Publisher Copyright: {\textcopyright} 2024 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.",
year = "2024",
month = aug,
doi = "10.1002/pro.5087",
language = "אנגלית",
volume = "33",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell",
number = "8",
}