Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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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)
  • Received : 2016.10.07
  • Accepted : 2016.11.14
  • Published : 2017.03.28
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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.

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