Literature DB >> 7906229

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

D Peralta1, D J Hartman, N J Hoogenraad, P B Høj.   

Abstract

Pig heart mitochondrial malate dehydrogenase was chemically denatured in guanidine HCl. Upon 50-fold dilution of the denaturant spontaneous refolding could be observed in the temperature range 12-32 degrees C. At 36 degrees C spontaneous refolding was not observed but a stable folding intermediate that is fairly resistant to aggregation was formed. This intermediate is readily refolded by the chaperonins GroEL and GroES and may prove useful in future attempts to describe several aspects of chaperonin action at physiological temperatures.

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Year:  1994        PMID： 7906229     DOI： 10.1016/0014-5793(94)80381-1

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


  13 in total

1.  Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.

Authors:  Y Dubaquié; R Looser; S Rospert
Journal:  Proc Natl Acad Sci U S A       Date:  1997-08-19       Impact factor: 11.205

Review 2.  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

3.  beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.

Authors:  P Gervasoni; W Staudenmann; P James; P Gehrig; A Plückthun
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-29       Impact factor: 11.205

4.  GroEL-GroES-mediated protein folding requires an intact central cavity.

Authors:  J D Wang; M D Michelitsch; J S Weissman
Journal:  Proc Natl Acad Sci U S A       Date:  1998-10-13       Impact factor: 11.205

5.  Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.

Authors:  M J Todd; G H Lorimer; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  1996-04-30       Impact factor: 11.205

6.  Recognition of partially-folded mitochondrial malate dehydrogenase by GroEL. Steady and time-dependent emission anisotropy measurements.

Authors:  J E Churchich
Journal:  Protein Sci       Date:  1998-12       Impact factor: 6.725

7.  The effect of macromolecular crowding on chaperonin-mediated protein folding.

Authors:  J Martin; F U Hartl
Journal:  Proc Natl Acad Sci U S A       Date:  1997-02-18       Impact factor: 11.205

8.  Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL.

Authors:  Z Lin; E Eisenstein
Journal:  Proc Natl Acad Sci U S A       Date:  1996-03-05       Impact factor: 11.205

9.  Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5.

Authors:  J Chen; D L Smith
Journal:  Protein Sci       Date:  2001-05       Impact factor: 6.725

10.  Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement.

Authors:  P A Voziyan; M T Fisher
Journal:  Protein Sci       Date:  2000-12       Impact factor: 6.725
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