References on GroEL 


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Asymmetry of the GroEL-GroES Complex under Physiological Conditions as Revealed by Small-Angle X-Ray Scattering

Tomonao Inobe, Kazunobu Takahashi, Kosuke Maki, Sawako Enoki, Kiyoto Kamagata, Akio Kadooka, Munehito Arai, and Kunihiro Kuwajima

Biophys. J. 94: 1392-1402 (2008) (PDF File)






Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner

Yakov Kipnis, Niv Papo, Gilad Haran, and Amnon Horovitz

Proc. Natl. Acad. Sci. USA 104:3119-3124 (2007). (PDF File)






Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding

Bei-Wen Ying, Hideki Taguchi, and Takuya Ueda

J. Biol. Chem. 281(31):21813-21819 (2006). (PDF File)


GroEL-GroES-mediated protein folding

Arthur L. Horwich, George W. Farr, and Wayne A. Fenton

Chem. Rev. 106:1917-1930 (2006).  (PDF File)


Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL

Ayumi Koike-Takeshita, Tatsuro Shimamura, Ken Yokoyama, Masasuke Yoshida, and Hideki Taguchi

J. Biol. Chem. 281:962-967 (2006) (PDF File)



Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operates as a "two-stroke engine"

Ryo Iizuka, Takao Yoshida, Moriyuki Ishii, Tamotsu Zako, Kazunobu Takahashi, Kosuke maki, Tomonao Inobe, Kunihiro Kuwajima, and Masafumi Yohda

J. Biol. Chem. 280(48):40375-40383 (2005). (PDF File


Chaperonin GroEL meets the substrate protein as a "Load of the Rings"

Hideki Taguchi

J. Biochem. 137:543-549 (2005) (PDF File)


Single-molecule fluorescence spectroscopy of protein folding

Benjamin Schuler

ChemPhysChem 6:1206-1220 (2005). (PDF File)


The 13Structure of a Chaperonin GroEL-Protein Substrate Complex by Cryo-electron Microscopy

S. Falke, F. Tama, C.L. Brooks III, E.P. Gogol and M.T. Fisher

J. Mol. Biol. 348:219-230 (2005). (PDF File)


Asymmetric binding of membrane proteins to GroEL

Jinhchuan Sun, Christos G. Savva, John Deaton, H. Ronald Kaback, Maja Svrakic, Ry Ypung, and Andreas Holzenburg

Arch. Biochem. Biophys. 434:352-357 (2005). (PDF File)


Allosteric regulation of chaperonins

Amnon Horovitz, and Keith R. Willison

Current Opinion Struct. Biol. 15:646-651 (2005). (PDF File)




Crystal structure of the native Chaperonin complex from thermus thermophilus reviealed unexpected asymmetry at the cis-cavity

Tatsuro Shimamura, Ayumi Koike-Takeshita, Ken Yokoyama, Ryoji Masui, Noriyuki Murai, Masasuke Yoshida, Hideki Taguchi, and So Iwata

Structure 12:1471-1480 (2004). (PDF FIle)


GroEL Mediates Protein Folding with a Two Successive Timer Mechanism

Taro Ueno, Hideki Taguchi, Hisashi Tadakuma, Masasuke Yoshida, and Takashi Funatsu

Molecular Cell 14:423–434 (2004). (PDF File)


A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive disscoation

B Trevor Sewell, Robert B Best, Shaoxia Chen, Alan M Roseman, Geoge W Farr, Arthur L. Horwich and Helen R. Saibil

Nature Struct. Mol. Biol. 11:1128–1133 (2004). (PDF File)


Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL

Fumihiro Motojima, Charu chaudhry, Wayne A. Fenton, George W. Farr, and Arthur L. Horwich

Proc. Natl. Acad. Sci. USA 101(42):15005-15012 (2004). (PDF File)


Single molecule imaging of protein folding mediated by chaperonin GroEL

Taro Ueno

Thesis (Waseda University) (2004). (PDF File)



Chaperonin-mediated protein folding: fate of substrate polypeptide

Wayne A. Fenton and Arthur L. Horwich

Quarterly Reviews of Biophysics 36(2):229-256 (2003). (PDF File)


Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics

Charu chaudhry, George W. Farr, Matthew J. Todd, Hays S. Rye, Axel T. Brunger, Paul D. Adams, Arthur L. Horwich, and Paul B. Sigler

EMBO J. 22(19):4877-4887 (2003). (PDF File)






Synchronized Domain-opening Motion of GroEL is Essential for Communication between the Two Rings

K. Shiseki, N. Murai, F. Motojima, T. Hisabori, M. Yoshida, and H. Taguchi

J. Biol. Chem. 276(14):11335-11338 (2001). (PDF File


Single-molecule observation of protein–protein interactions in the chaperonin system

Hideki Taguchi, Taro Ueno, Hisashi Tadakuma, Masasuke Yoshida, Takashi Funatsu

Nature Biotech.19:861-865 (2001). (PDF File)


GroEL/GroES-mediated folding of a protein too large to be encapsulated

Tapan K. Cahudhuri, George W. Farr, Wayne A. Fenton, Sabine Rospert, and Arthur L. Horwich

Cell 107:235-246 (2001). (PDF File)


Review: Allosteyr in Chaperonins

Amnon Horvitz, Yael Fridmann, Calit Kafri, and Ofer Yifrach

J. Struct. Biol. 135:104-114 (2001). (PDF File)


Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1

Kafri, G., Willison KR, and Horovitz A

Protein Sci. 10:445-449 (2001). (PDF File)


Dual function of protein confinement in chaperonin-assisted protein folding

Achim Brinker, Guenther Pfeifer, Michael J. Kerner, Dean J. Naylor, F. Ulrich Hartl, and Manajit Hayer-Hartl

Cell 107: 223-233 (2001) (PDF File)


Review: A Structural View of the GroEL Chaperone Cycle

Holger Grallert and Johannes Buchner

J. Struct. Biol. 135:95-103 (2001). (PDF File)





A Dynamic Model for the Allosteric Mechnism of GroEL

J. Ma, P.B. Sigler, Z. Xu and M. Karplus

J. Mol. Biol. 302:303-313 (2000). (PDF File)


Probing protein-protein interactions in real time

Mario B. Viani, Lia I. Pietrasanta, James B. Thompson, Ami chand, Ilse C. Gebenshuber, Jhanness H. Kindt, Michael Richter, Helen G. Hansma and Paul K. Hansma

Nature Struct. Bio. 7(8):644-647 (2000). (PDF File)


Coupling between protein folding and allosttery in the GroE chaperonin system

O. Yifrach and . Horovitz

PNAS 97(4):1521-1524 (2000). (PDF File)


Limits of protein folding inside GroE complexes

Holger Grallert, Kerstin Rutkat, and Johannes Buchner

J. Biol. Chem. 275:20424-20430 (2000). (PDF File)



Prior to 2000


GroEL-GroES cycling: ATP and nonnative @olypeptide direct alternation of folding-active rings

hays S. Rye, Alan M. Roseman, Shaxia Chen, Krystyna  Furtak, Wayne A. Fenton, Helen R. Saibil, and Arthur L. Horwich

Cell 97:325-338 (1999). (PDF File)


Catalysis, commitment and encapsulation during GroE-mediated folding

Martina Beissinger, Kerstin Rutkat, and Johannes Buchner

J. Mol. Biol. 289:1075-1092 (1999). (PDF File)


The Hsp70 and HSP60 Chaperone Machines

Bernd Bukau and Arthur L. Horwich

Cell 92:351-366 (1998). (PDF File)


GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase

Holger Gralleret, Kerstin Rutkat, and Johannes Buchner

J. Biol. Chem. 273(50):33305-33310 (1998). (PDF File)


Asymmetry, commitment and inhibition in the GroE ATPase cycle impose altering functions on the two GroEL rings

Neil M. kad, Neil A. Ranson, Matthew J. Cliff and Anthony R. Clarke

J. Mol. Biol. 278:267-278 (1998). (PDF File)


Structure and function in GroEL-mediated protein folding

Paul B. Sigler, Zhaohui Xu, Hays S. Rye, Steven G. Burston, Wayne A. Fenton, and Arthur L. HorwichBernd Bukau and Arthur L. Horwich

Annu. Rev. Biochem. 67:581-608 (1998). (PDF File)


Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

Hays S. Rye, Steven G. Burston, Wayne A. Fenton, Joseph M. Beechem, Zhaohui Xu, Paul B. Sigler, and Arthur L. Horwich

Nature 388:792-798 (1997). (PDF File)


Catalysis of protein folding by symmetric chaperone complexes.

Sparrer H., Rutkat K., and Buchner J.

Proc. Natl. Acad. Sci. USA 94:1096-1100 (1997). (PDF File)


How GroES regulates binding of nonnative protein to GroEL

Helmut Sparrer and Johannes Buchner

J. Biol. Chem. 272(22):14080-14086 (1997). (PDF File)


The chaperonin ATPase cycle: mechanism of allosteric switching and movementts of substrate-binding domains in GroEL

Alan M. Roseman, Shaoxia Chen, Helen White, Kerstin Braig, and Helen R. Saibil

Cell 78:241-251 (1996). (PDF File)


Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL

Ofer Yifrach and Amnon Horovitz

Biochemistry 34(16):5303-5308 (1995). (PDF File)


Increased efficiency of GroE-assisted protein filding by manganese ions

Sophia Diamant, Abdussalam Azem, Celeste Weiss, and Pierre Goloubinoff

J. Biol. Chem. 270:28387-28391 (1995). (PDF File)


The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 Heterooligomer

A. Azem, S. Diamant, M. Kessel, C. Weiss, and P. Goloubinoff

Proc. Natl. Acad. Sci. USA 92:12021-12025 (1995). (PDF File)


Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes

Andreas Engel, Manajit K. Hayer-Hartl, Kenneth N. Goldie, Gunter Pfeifer, Reiner Hegerl, Shirley Muller, Ana C.R. da Silva, Wolfgang baumeister, F. Ulrich Hartl

Science 269:832-836 (1995). (PDF File)


Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding

Manajit K. Hayer-Hartl, Jorg Martin, and F. Ulrich Hartl

Science 269:836-841 (1995). (PDF File)


Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy

Shaoxia Chen, Alan M. Roseman, Alilson S. Hunter, Stephen P. Wood, Steven G. Burston, Neil A. Ranson, Anthony R. Clarke & Helen R. Saibil

Nature 371:261-264 (1994). (PDF File)