Skip Navigation

Journal of Biochemistry 2005 137(5):543-549; doi:10.1093/jb/mvi069
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Taguchi, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Taguchi, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2005 The Japanese Biochemical Society

JB Minireview

Chaperonin GroEL Meets the Substrate Protein as a "Load" of the Rings

Hideki Taguchi*

Graduate School of Frontier Sciences, University of Tokyo and PRESTO, Japan Science and Technology Agency, FSB401, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562

* For correspondence: Phone: +81-4-7136-3644, Fax: +81-4-7136-3644, E-mail: taguchi{at}k.u-tokyo.ac.jp

Chaperonin GroEL is an essential molecular chaperone that assists protein folding in the cell. With the aid of cochaperonin GroES and ATP, double ring-shaped GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex. Although extensive studies have revealed the outline of GroEL mechanism over the past decade, central questions remain: What are the in vivo substrate proteins? How does GroEL encapsulate the substrates inside the cavity in spite of an apparent entropic difficulty? Is the folding inside the GroEL-ES cavity the same as bulk spontaneous folding? In this review I summarize the recent progress on in vivo and in vitro aspects of GroEL. In particular, emerging evidence shows that the substrate protein itself influences the chaperonin GroEL structure and reaction cycle. Finally I propose the mechanistic similarity between GroEL and kinesin, a molecular motor that moves along a microtubule in an ATP-dependent manner.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
J. P. Grason, J. S. Gresham, L. Widjaja, S. C. Wehri, and G. H. Lorimer
Setting the chaperonin timer: The effects of K+ and substrate protein on ATP hydrolysis
PNAS, November 11, 2008; 105(45): 17334 - 17338.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. P. Grason, J. S. Gresham, and G. H. Lorimer
Setting the chaperonin timer: A two-stroke, two-speed, protein machine
PNAS, November 11, 2008; 105(45): 17339 - 17344.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Koike-Takeshita, M. Yoshida, and H. Taguchi
Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant
J. Biol. Chem., August 29, 2008; 283(35): 23774 - 23781.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B.-W. Ying, H. Taguchi, and T. Ueda
Co-translational Binding of GroEL to Nascent Polypeptides Is Followed by Post-translational Encapsulation by GroES to Mediate Protein Folding
J. Biol. Chem., August 4, 2006; 281(31): 21813 - 21819.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.