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KMID : 0545120170270030644
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Journal of Microbiology and Biotechnology
2017 Volume.27 No. 3 p.644 ~ p.647
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Interaction of a 22 kDa Peptidyl Prolyl cis/trans Isomerase with the Heat Shock Protein DnaK in Vibrio anguillarum
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Kang Dong-Seop
Moon Soo-Young
Cho Hwa-Jin
Lee Jong-Min
Kong In-Soo
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Abstract
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Peptidyl prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidylprolyl 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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KEYWORD
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Peptidyl prolyl cis/trans isomerase (PPIase), DnaK, protein-protein interaction, Vibrio anguillarum
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