Folding and assembly of the Escherichia coli succinyl-CoA synthetase heterotetramer without participation of molecular chaperones.
Succinyl-CoA synthetase of Escherichia coli (alpha 2B2 subunit structure) has been shown to fold and assemble without participation by molecular chaperones. Renaturation experiments showed that purified bacterial chaperone GroEL has no effect on the folding and assembly of the active tetrameric enzyme. When isolated 35S-labeled alpha or beta subunits were incubated with GroEL in the absence of ATP, there was no complex formation between the subunits and GroEL. These in vitro results were confirmed by in vivo analysis of the folding and assembly of newly synthesized succinyl-CoA synthetase subunits. When expression of the subunits was induced in E. coli strains that bear GroEL or GroES temperature-sensitive mutations, the assembly of active succinyl-CoA synthetase was not affected as the temperature was raised to 43 degrees C. These and other observations are discussed that indicate that folding and assembly of succinyl-CoA synthetase may be independent of assistance by any chaperone.
Fong
G
G
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Bridger
W A
WA
D001426:Bacterial Proteins / Q000378:metabolism*; D018834:Chaperonin 60; D004926:Escherichia coli / Q000201:enzymology; D006360:Heat-Shock Proteins / Q000378:metabolism*; D046911:Macromolecular Substances; D011485:Protein Binding; D011487:Protein Conformation; D013389:Succinate-CoA Ligases / Q000378:metabolism / Q000648:ultrastructure*
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D046911:Macromolecular Substances; D013389:Succinate-CoA Ligases