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

D Peralta; D J Hartman; N J Hoogenraad; P B Høj

doi:10.1016/0014-5793(94)80381-1

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

FEBS Lett. 1994 Feb 14;339(1-2):45-9. doi: 10.1016/0014-5793(94)80381-1.

Authors

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

Affiliation

¹ Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.

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

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenosine Triphosphate / pharmacology
Animals
Bacterial Proteins / pharmacology*
Chaperonin 10
Chaperonin 60
Escherichia coli / chemistry
Guanidine
Guanidines
Heat-Shock Proteins / pharmacology*
Macromolecular Substances
Malate Dehydrogenase / chemistry*
Mitochondria, Heart / enzymology*
Protein Denaturation
Protein Folding*
Swine
Temperature

Substances

Bacterial Proteins
Chaperonin 10
Chaperonin 60
Guanidines
Heat-Shock Proteins
Macromolecular Substances
Adenosine Triphosphate
Malate Dehydrogenase
Guanidine