GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL.
The presence of GroEL/ES during the refolding of human carbonic anhydrase II (pseudo-wild type) was found to increase the yield of active enzyme from 65 to 100%. This chaperone action on the enzyme could be obtained by adding GroEL alone, and the time-course in that case was only moderately slower than the spontaneous process. Truncated forms of carbonic anhydrase, in which N-terminal helices were removed, also served as protein substrates for GroEL/ES. This demonstrates that N-terminally located helices are not obligatory as recognition motifs.
Persson
M
M
IFM-Department of Chemistry, Linköping University, Sweden.
Aronsson
G
G
Bergenhem
N
N
Freskgård
P O
PO
Jonsson
B H
BH
Surin
B P
BP
Spangfort
M D
MD
Carlsson
U
U
D001665:Binding Sites; D002256:Carbonic Anhydrases / Q000737:chemistry*; D018835:Chaperonin 10 / Q000494:pharmacology*; D018834:Chaperonin 60 / Q000494:pharmacology*; D004793:Enzyme Reactivators / Q000494:pharmacology*; D006801:Humans; D017510:Protein Folding
D018835:Chaperonin 10; D018834:Chaperonin 60; D004793:Enzyme Reactivators; D002256:Carbonic Anhydrases