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- Title
Chaperonin facilitates protein folding by avoiding initial polypeptide collapse.
- Authors
Motojima, Fumihiro; Fujii, Katsuya; Yoshida, Masasuke
- Abstract
Chaperonins assist folding of many cellular proteins, including essential proteins for cell viability. However, it remains unclear how chaperonin-assisted folding is different from spontaneous folding. Chaperonin GroEL/GroES facilitates folding of denatured protein encapsulated in its central cage but the denatured protein often escapes from the cage to the outside during reaction. Here, we show evidence that the in-cage-folding and the escape occur diverging from the same intermediate complex in which polypeptide is tethered loosely to the cage and partly protrudes out of the cage. Furthermore, denatured proteins in the chaperonin cage are kept in more extended conformation than those initially formed in spontaneous folding. We propose that the formation of tethered intermediate of polypeptide is necessary to prevent polypeptide collapse at the expense of polypeptide escape. The tethering of polypeptide would allow freely mobile portions of tethered polypeptide to fold segmentally.
- Subjects
MOLECULAR chaperones; PROTEIN folding; POLYPEPTIDES; UBIQUITIN; ENCAPSULATION (Catalysis)
- Publication
Journal of Biochemistry, 2018, Vol 164, Issue 5, p369
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/jb/mvy061