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Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
J Mol Biol. 2015 Sep 11; 427(18):2912-8.JM

Abstract

Chaperonin GroEL is an essential chaperone that assists in protein folding in the cell. Since one GroEL ring binds one GroES heptamer, the GroEL double ring permits the formation of two types of GroEL:GroES complexes: asymmetric 1:1 "bullet"-shaped and symmetric 1:2 "football"-shaped GroEL:GroES2 complexes. There have been continuing debates about the mechanism and which complex is critical to the chaperonin-assisted folding. In this review, I summarize the recent progress on the football complex.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Taguchi H
Department of Biomolecular Engineering, Graduate School of Biosciences and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan. Electronic address: taguchi@bio.titech.ac.jp.

MeSH

Adenosine TriphosphateChaperonin 10Chaperonin 60ChaperoninsEscherichia coliFluorescence Resonance Energy TransferProtein BindingProtein ConformationProtein FoldingSubstrate Specificity

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

25900372

Citation

Taguchi, Hideki. "Reaction Cycle of Chaperonin GroEL Via Symmetric "Football" Intermediate." Journal of Molecular Biology, vol. 427, no. 18, 2015, pp. 2912-8.
Taguchi H. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate. J Mol Biol. 2015;427(18):2912-8.
Taguchi, H. (2015). Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate. Journal of Molecular Biology, 427(18), 2912-8. https://doi.org/10.1016/j.jmb.2015.04.007
Taguchi H. Reaction Cycle of Chaperonin GroEL Via Symmetric "Football" Intermediate. J Mol Biol. 2015 Sep 11;427(18):2912-8. PubMed PMID: 25900372.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate. A1 - Taguchi,Hideki, Y1 - 2015/04/18/ PY - 2015/03/03/received PY - 2015/04/12/revised PY - 2015/04/14/accepted PY - 2015/4/23/entrez PY - 2015/4/23/pubmed PY - 2015/12/15/medline KW - GroEL KW - Hsp60 KW - chaperone KW - chaperonin KW - protein folding SP - 2912 EP - 8 JF - Journal of molecular biology JO - J Mol Biol VL - 427 IS - 18 N2 - Chaperonin GroEL is an essential chaperone that assists in protein folding in the cell. Since one GroEL ring binds one GroES heptamer, the GroEL double ring permits the formation of two types of GroEL:GroES complexes: asymmetric 1:1 "bullet"-shaped and symmetric 1:2 "football"-shaped GroEL:GroES2 complexes. There have been continuing debates about the mechanism and which complex is critical to the chaperonin-assisted folding. In this review, I summarize the recent progress on the football complex. SN - 1089-8638 UR - https://www.unboundmedicine.com/medline/citation/25900372/Reaction_Cycle_of_Chaperonin_GroEL_via_Symmetric_"Football"_Intermediate_ DB - PRIME DP - Unbound Medicine ER -