Literature DB >> 1348056

Positive cooperativity in the functioning of molecular chaperone GroEL.

E S Bochkareva1, N M Lissin, G C Flynn, J E Rothman, A S Girshovich.   

Abstract

In the presence of its partner, GroES, the tetradecameric molecular chaperone GroEL binds 14 ATP molecules, half of which are hydrolyzed in a cooperative manner. Moreover GroEL can bind, with a positive cooperativity, more than two molecules of nonfolded protein rhodanese. The role of the cooperative mechanism in the functioning of GroEL is discussed.

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Year:  1992        PMID: 1348056

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  31 in total

Review 1.  Chaperone rings in protein folding and degradation.

Authors:  A L Horwich; E U Weber-Ban; D Finley
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

2.  Alternating translocation of protein substrates from both ends of ClpXP protease.

Authors:  Joaquin Ortega; Hyun Sook Lee; Michael R Maurizi; Alasdair C Steven
Journal:  EMBO J       Date:  2002-09-16       Impact factor: 11.598

3.  Thermal denaturation of Bungarus fasciatus acetylcholinesterase: Is aggregation a driving force in protein unfolding?

Authors:  I Shin; E Wachtel; E Roth; C Bon; I Silman; L Weiner
Journal:  Protein Sci       Date:  2002-08       Impact factor: 6.725

Review 4.  Regulation by proteolysis: energy-dependent proteases and their targets.

Authors:  S Gottesman; M R Maurizi
Journal:  Microbiol Rev       Date:  1992-12

Review 5.  GroEL-mediated protein folding: making the impossible, possible.

Authors:  Zong Lin; Hays S Rye
Journal:  Crit Rev Biochem Mol Biol       Date:  2006 Jul-Aug       Impact factor: 8.250

6.  Capture of monomeric refolding intermediate of human muscle creatine kinase.

Authors:  Sen Li; Ji-Hong Bai; Yong-Doo Park; Hai-Meng Zhou
Journal:  Protein Sci       Date:  2006-01       Impact factor: 6.725

7.  Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.

Authors:  F J Corrales; A R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  1996-04-30       Impact factor: 11.205

8.  The allosteric mechanism of the chaperonin GroEL: a dynamic analysis.

Authors:  J Ma; M Karplus
Journal:  Proc Natl Acad Sci U S A       Date:  1998-07-21       Impact factor: 11.205

9.  The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.

Authors:  B C Freeman; R I Morimoto
Journal:  EMBO J       Date:  1996-06-17       Impact factor: 11.598

10.  Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.

Authors:  Tomoya Sameshima; Taro Ueno; Ryo Iizuka; Noriyuki Ishii; Naofumi Terada; Kohki Okabe; Takashi Funatsu
Journal:  J Biol Chem       Date:  2008-06-20       Impact factor: 5.157

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