Abstract:
:In the presence of ADP, the molecular chaperones GroEL and GroES from Escherichia coli not only facilitated the refolding of various proteins, but also prevented their irreversible heat inactivation in vitro. Without nucleotides the refolding reactions were arrested by GroEL. Addition of GroES and ADP to the reaction mixture initiated the refolding reactions and the enzyme activities were regained efficiently. The presence of GroE (GroEL and GroES) and ADP also protected against heat inactivation of native enzymes at various temperatures. These findings suggest that in the presence of GroES, nucleotide binding is an important event in the mechanism of GroEL-facilitated protein folding.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kawata Y,Nosaka K,Hongo K,Mizobata T,Nagai Jdoi
10.1016/0014-5793(94)00456-0subject
Has Abstractpub_date
1994-05-30 00:00:00pages
229-32issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(94)00456-0journal_volume
345pub_type
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