Literature DB >> 20083109

ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle.

Navneet K Tyagi1, Wayne A Fenton, Arthur L Horwich.   

Abstract

The GroEL/GroES protein folding chamber is formed and dissociated by ATP binding and hydrolysis. ATP hydrolysis in the GroES-bound (cis) ring gates entry of ATP into the opposite unoccupied trans ring, which allosterically ejects cis ligands. While earlier studies suggested that hydrolysis of cis ATP is the rate-limiting step of the cycle (t1/2 approximately 10 s), a recent study suggested that ADP release from the cis ring may be rate-limiting (t1/2 approximately 15-20 s). Here we have measured ADP release using a coupled enzyme assay and observed a t1/2 for release of <or=4-5 s, indicating that this is not the rate-limiting step of the reaction cycle. Copyright (c) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20083109      PMCID: PMC2849271          DOI: 10.1016/j.febslet.2010.01.021

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


  19 in total

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

Authors:  Fumihiro Motojima; Charu Chaudhry; Wayne A Fenton; George W Farr; Arthur L Horwich
Journal:  Proc Natl Acad Sci U S A       Date:  2004-10-12       Impact factor: 11.205

Review 2.  Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding.

Authors:  Arthur L Horwich; Wayne A Fenton
Journal:  Q Rev Biophys       Date:  2009-07-29       Impact factor: 5.318

3.  Triggering protein folding within the GroEL-GroES complex.

Authors:  Damian Madan; Zong Lin; Hays S Rye
Journal:  J Biol Chem       Date:  2008-09-09       Impact factor: 5.157

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

Authors:  A M Roseman; S Chen; H White; K Braig; H R Saibil
Journal:  Cell       Date:  1996-10-18       Impact factor: 41.582

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

Authors:  N M Kad; N A Ranson; M J Cliff; A R Clarke
Journal:  J Mol Biol       Date:  1998-04-24       Impact factor: 5.469

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

Authors:  H S Rye; S G Burston; W A Fenton; J M Beechem; Z Xu; P B Sigler; A L Horwich
Journal:  Nature       Date:  1997-08-21       Impact factor: 49.962

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 origins and consequences of asymmetry in the chaperonin reaction cycle.

Authors:  S G Burston; N A Ranson; A R Clarke
Journal:  J Mol Biol       Date:  1995-05-26       Impact factor: 5.469

9.  GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.

Authors:  H S Rye; A M Roseman; S Chen; K Furtak; W A Fenton; H R Saibil; A L Horwich
Journal:  Cell       Date:  1999-04-30       Impact factor: 41.582

10.  Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.

Authors:  J S Weissman; H S Rye; W A Fenton; J M Beechem; A L Horwich
Journal:  Cell       Date:  1996-02-09       Impact factor: 41.582

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  2 in total

1.  Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.

Authors:  Xiang Ye; George H Lorimer
Journal:  Proc Natl Acad Sci U S A       Date:  2013-10-28       Impact factor: 11.205

2.  Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics.

Authors:  Ningzi Guan; Hyun-dong Shin; Rachel R Chen; Jianghua Li; Long Liu; Guocheng Du; Jian Chen
Journal:  Sci Rep       Date:  2014-11-07       Impact factor: 4.379

  2 in total

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