Reconciling the controversy regarding the functional importance of bullet- and football-shaped GroE complexes

The chaperonin GroEL and its co-chaperonin GroES form both GroEL–GroES bullet-shaped and GroEL–GroES2 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 com...

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Bibliographic Details
Published in:The Journal of biological chemistry 2019-09, Vol.294 (37), p.13527-13529
Main Authors: Bigman, Lavi S., Horovitz, Amnon
Format: Article
Language:English
Subjects:
Accelerated Communications
bioinformatics
chaperonin
Chaperonin 10 - metabolism
Chaperonin 10 - physiology
Chaperonin 60 - metabolism
Chaperonin 60 - physiology
Chaperonins - metabolism
Escherichia coli - metabolism
Escherichia coli Proteins - metabolism
Escherichia coli Proteins - physiology
Fluorescence Resonance Energy Transfer - methods
GroEL
Heat-Shock Proteins - metabolism
Heat-Shock Proteins - physiology
kinetics
molecular machines
Protein Binding
Protein Folding
PSIPRED
Structure-Activity Relationship
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Summary:The chaperonin GroEL and its co-chaperonin GroES form both GroEL–GroES bullet-shaped and GroEL–GroES2 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.AC119.010299