期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 294, 期 37, 页码 13527-13529出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.AC119.010299
关键词
chaperonin; protein folding; GroEL; kinetics; bioinformatics; molecular machines; PSIPRED
资金
- United States-Israel Binational Science Foundation [2015170]
- Minerva Foundation
- Federal German Ministry for Education and Research
- Kimmelman Center for Biomolecular Structure and Assembly
The chaperonin GroEL and its co-chaperonin GroES form both GroEL-GroES bullet-shaped and GroEL-GroES(2) football-shaped complexes. The residence time of protein substrates in the cavities of these complexes is about 10 and 1 s, respectively. There has been much controversy regarding which of these complexes is the main functional form. Here, we show using computational analysis that GroEL protein substrates have a bimodal distribution of folding times, which matches these residence times, thereby suggesting that both bullet-shaped and football-shaped complexes are functional. More generally, co-existing complexes with different stoichiometries are not mutually exclusive with respect to having a functional role and can complement each other.
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