| Literature DB >> 12628000 |
Andrew R Kusmierczyk1, Jörg Martin.
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.Entities:
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Year: 2003 PMID: 12628000 PMCID: PMC1223359 DOI: 10.1042/BJ20030230
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857