3 years ago

Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains

Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains
Xiao-Wei Wang, Wen-Bin Zhang
Catenanes are intriguing molecular architectures with unique properties. Herein, we report the cellular synthesis of protein catenanes containing folded structural domains, aided by synergy between p53 dimerization and SpyTag/SpyCatcher chemistry. Concatenation of green fluorescent protein (GFP) was shown to increase chemical stability without disrupting the fluorescence properties, and concatenated dihydrofolate reductase (DHFR) exhibited a melting temperature around 4 °C higher and catalytic activity around 27 % higher than the wild-type DHFR and the cyclic/linear controls. Catenation also confers considerable proteolytic resistance on DHFR. The results suggest that catenation could enhance both the stability and activity of folded proteins, thus making topology engineering an attractive approach for tailoring protein properties without varying their native sequences. We go together: Cellular synthesis of protein catenanes containing folded structural domains was effectively achieved by using p53 dimerization and SpyTag/SpyCatcher chemistry. Catenation was found to endow the purified proteins of interest (POIs) with several valuable attributes, including enhanced thermal stability, increased proteolytic resistance, and enhanced enzymatic activity.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201705194

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