Nucleotide-dependent protein folding in the type II chaperonin from the 
mesophilic archaeon Methanococcus maripaludis

Kusmierczyk, AR; Martin, J

doi:10.1042/BJ20030230

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Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis

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Martin, J
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Kusmierczyk, A., & Martin, J. (2003). Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis. Biochemical Journal, 371(3), 669-673. doi:10.1042/BJ20030230.

Cite as: https://hdl.handle.net/21.11116/0000-000B-623D-3

Abstract

We report the characterization of the first chaperonin (Mm-cpn) from a mesophilic archaeon, Methanococcus maripaludis. The single gene was cloned from genomic DNA and expressed in Escherichia coli to produce a recombinant protein of 543 amino acids. In contrast with other known archaeal chaperonins, Mm-cpn is fully functional in all respects under physiological conditions of 37 degrees C. The complex has Mg(2+)-dependent ATPase activity and can prevent the aggregation of citrate synthase. It promotes a high-yield refolding of guanidinium-chloride-denatured rhodanese in a nucleotide-dependent manner. ATP binding is sufficient to effect folding, but ATP hydrolysis is not essential.