The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding Journal Article

  

Authors:	Martin, J.; Mayhew, M.; Langer, T.; Hartl, F. U.
Article Title:	The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
Abstract:	The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded polypeptide within the cavity of the GroEL cylinder triggers ADP and GroES release. Upon ADP-ATP exchange, GroES reassociates with GroEL and ATP hydrolysis discharges the bound protein for folding. Partially folded protein rebinds to the chaperonin, thus perpetuating the cycle until folding is complete. © 1993 Nature Publishing Group.
Keywords:	nonhuman; protein conformation; models, biological; protein binding; protein interaction; adenosine diphosphate; bacterial proteins; escherichia coli; adenosine triphosphate; protein folding; reaction analysis; nucleotides; cross-linking reagents; heat-shock proteins; succinimides; priority journal; article; support, non-u.s. gov't; chaperonin; groel protein; groes protein
Journal Title:	Nature
Volume:	366
Issue:	6452
ISSN:	0028-0836
Publisher:	Nature Publishing Group
Date Published:	1993-11-18
Start Page:	228
End Page:	233
Language:	English
DOI:	10.1038/366228a0
PUBMED:	7901770
PROVIDER:	scopus
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027427326&doi=10.1038%2f366228a0&partnerID=40&md5=5b30006e7df7ff9beb54dde7f9c6efc0
Notes:	Article -- Export Date: 1 March 2019 -- Source: Scopus

https://synapse.mskcc.org/synapse/works/has_related_data_chk/144278