Literature DB >> 19577567

The GroEL/GroES cis cavity as a passive anti-aggregation device.

Arthur L Horwich1, Adrian C Apetri, Wayne A Fenton.   

Abstract

The GroEL/GroES chaperonin folding chamber is an encapsulated space of approximately 65 A diameter with a hydrophilic wall, inside of which many cellular proteins reach the native state. The question of whether the cavity wall actively directs folding reactions or is playing a passive role has been open. We review past and recent observations and conclude that the chamber functions as a passive "Anfinsen cage" that prevents folding monomers from multimolecular aggregation.

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Year:  2009        PMID： 19577567      PMCID： PMC2759771          DOI： 10.1016/j.febslet.2009.06.049

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  48 in total

1.  ATP-bound states of GroEL captured by cryo-electron microscopy.

Authors:  N A Ranson; G W Farr; A M Roseman; B Gowen; W A Fenton; A L Horwich; H R Saibil
Journal:  Cell       Date:  2001-12-28       Impact factor: 41.582

2.  Dual function of protein confinement in chaperonin-assisted protein folding.

Authors:  A Brinker; G Pfeifer; M J Kerner; D J Naylor; F U Hartl; M Hayer-Hartl
Journal:  Cell       Date:  2001-10-19       Impact factor: 41.582

Review 3.  Molecular chaperones in the cytosol: from nascent chain to folded protein.

Authors:  F Ulrich Hartl; Manajit Hayer-Hartl
Journal:  Science       Date:  2002-03-08       Impact factor: 47.728

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

Authors:  Charu Chaudhry; George W Farr; Matthew J Todd; Hays S Rye; Axel T Brunger; Paul D Adams; Arthur L Horwich; Paul B Sigler
Journal:  EMBO J       Date:  2003-10-01       Impact factor: 11.598

5.  Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

Authors:  Yun-Chi Tang; Hung-Chun Chang; Annette Roeben; Dirk Wischnewski; Nadine Wischnewski; Michael J Kerner; F Ulrich Hartl; Manajit Hayer-Hartl
Journal:  Cell       Date:  2006-06-02       Impact factor: 41.582

Review 6.  Two families of chaperonin: physiology and mechanism.

Authors:  Arthur L Horwich; Wayne A Fenton; Eli Chapman; George W Farr
Journal:  Annu Rev Cell Dev Biol       Date:  2007       Impact factor: 13.827

7.  Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction.

Authors:  N A Ranson; S G Burston; A R Clarke
Journal:  J Mol Biol       Date:  1997-03-07       Impact factor: 5.469

8.  The crystal structure of the GroES co-chaperonin at 2.8 A resolution.

Authors:  J F Hunt; A J Weaver; S J Landry; L Gierasch; J Deisenhofer
Journal:  Nature       Date:  1996-01-04       Impact factor: 49.962

9.  Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.

Authors:  Eun Sun Park; Wayne A Fenton; Arthur L Horwich
Journal:  Proc Natl Acad Sci U S A       Date:  2007-02-05       Impact factor: 11.205

10.  Residue lysine-34 in GroES modulates allosteric transitions in GroEL.

Authors:  O Kovalenko; O Yifrach; A Horovitz
Journal:  Biochemistry       Date:  1994-12-20       Impact factor: 3.162
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  32 in total

1.  Expression and functional characterization of the first bacteriophage-encoded chaperonin.

Authors:  Lidia P Kurochkina; Pavel I Semenyuk; Victor N Orlov; Johan Robben; Nina N Sykilinda; Vadim V Mesyanzhinov
Journal:  J Virol       Date:  2012-07-11       Impact factor: 5.103

2.  Archaeal-like chaperonins in bacteria.

Authors:  Stephen M Techtmann; Frank T Robb
Journal:  Proc Natl Acad Sci U S A       Date:  2010-11-05       Impact factor: 11.205

3.  The N-terminal domain of Aliivibrio fischeri LuxR is a target of the GroEL chaperonin.

Authors:  Ilya V Manukhov; Ol'ga E Melkina; Ignatii I Goryanin; Ancha V Baranova; Gennadii B Zavilgelsky
Journal:  J Bacteriol       Date:  2010-08-20       Impact factor: 3.490

4.  Putting handcuffs on the chaperonin GroEL.

Authors:  Amnon Horovitz
Journal:  Proc Natl Acad Sci U S A       Date:  2013-06-19       Impact factor: 11.205

Review 5.  Reconciling theories of chaperonin accelerated folding with experimental evidence.

Authors:  Andrew I Jewett; Joan-Emma Shea
Journal:  Cell Mol Life Sci       Date:  2009-10-23       Impact factor: 9.261

Review 6.  Integrating protein homeostasis strategies in prokaryotes.

Authors:  Axel Mogk; Damon Huber; Bernd Bukau
Journal:  Cold Spring Harb Perspect Biol       Date:  2011-04-01       Impact factor: 10.005

7.  Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.

Authors:  So Ishino; Yasushi Kawata; Hideki Taguchi; Naoko Kajimura; Katsumi Matsuzaki; Masaru Hoshino
Journal:  J Biol Chem       Date:  2015-04-17       Impact factor: 5.157

Review 8.  The chaperone toolbox at the single-molecule level: From clamping to confining.

Authors:  Mario J Avellaneda; Eline J Koers; Mohsin M Naqvi; Sander J Tans
Journal:  Protein Sci       Date:  2017-04-20       Impact factor: 6.725

9.  GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.

Authors:  Florian Georgescauld; Kristina Popova; Amit J Gupta; Andreas Bracher; John R Engen; Manajit Hayer-Hartl; F Ulrich Hartl
Journal:  Cell       Date:  2014-05-08       Impact factor: 41.582

10.  Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme.

Authors:  John W Lamppa; Sam A Tanyos; Karl E Griswold
Journal:  J Biotechnol       Date:  2012-12-07       Impact factor: 3.307
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