Abstract
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.
Original language | English |
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Pages (from-to) | 13527-13529 |
Number of pages | 3 |
Journal | Journal of Biological Chemistry |
Volume | 294 |
Issue number | 37 |
DOIs | |
State | Published - 13 Sep 2019 |