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http://dx.doi.org/10.4014/jmb.1610.10017

Interaction of a 22 kDa Peptidyl Prolyl cis/trans Isomerase with the Heat Shock Protein DnaK in Vibrio anguillarum  

Kang, Dong Seop (Department of Biotechnology, Pukyong National University)
Moon, Soo Young (Department of Biotechnology, Pukyong National University)
Cho, Hwa Jin (Department of Biotechnology, Pukyong National University)
Lee, Jong Min (Department of Biotechnology, Pukyong National University)
Kong, In-Soo (Department of Biotechnology, Pukyong National University)
Publication Information
Journal of Microbiology and Biotechnology / v.27, no.3, 2017 , pp. 644-647 More about this Journal
Abstract
Peptidyl prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds preceding prolines. We investigated the protein-protein interaction between a 22 kDa PPIase (VaFKBP22, an FK506-binding protein) and the molecular chaperone DnaK derived from Vibrio anguillarum O1 (VaDnaK) using GST pull-down assays and a bacterial two-hybrid system for in vivo and in vitro studies, respectively. Furthermore, we analyzed the three-dimensional structure of the protein-protein interaction. Based on our results, VaFKBP22 appears to act as a cochaperone of VaDnaK, and contributes to protein folding and stabilization via its peptidyl-prolyl cis/trans isomerization activity.
Keywords
Peptidyl prolyl cis/trans isomerase (PPIase); DnaK; protein-protein interaction; Vibrio anguillarum;
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