Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
2. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
3. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor.
4. GroE facilitates refolding of citrate synthase by suppressing aggregation
5. Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent
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