Fusion with heat-resistant obscure (Hero) proteins have the potential to improve the molecular property of recombinant proteins
Heroタンパク質が、目的タンパク質の可溶化・安定化融合タグとして応用可能なことを明らかにした。(現在、本論文およびPLOS Biol. 2020の知見と合わせ、GTIE GAPファンドによってスタートアップを目指した実証実験を行っている。)
Although recombinant proteins are widely used in biotechnology and pharmaceutical industries, improving their solubility and stability is often a challenging issue. We recently discovered a class of highly unstructured heat-resistant obscure (Hero) proteins, which function to protect other “client” proteins in trans from various stresses in vitro and in vivo. Here, we show that fusion of Hero proteins in cis can enhance the molecular property of recombinant proteins. Fusion with Hero11 improved the otherwise challenging production of TAR DNA-binding protein of 43 kDa (TDP-43) in Escherichia coli. Moreover, fusing with Hero9 strongly protected the activity of firefly luciferase bearing destabilizing mutations against heat and other stress conditions. These data suggest that Hero proteins have the potential to be used as versatile stabilization tags for recombinant protein production.
Authors: Morimoto E, Tsuboyama K, Tomari Y
Journal: PLoS One.2022 ;17(6):e0270097.
投稿者プロフィール
最新の投稿
令和6年度(FY2024)2025.01.23miRNA-mediated gene silencing in Drosophila larval development involves GW182-dependent and independent mechanisms
令和6年度(FY2024)2025.01.23The dual role of Spn-E in supporting heterotypic ping-pong piRNA amplification in silkworms
令和6年度(FY2024)2025.01.23DNAJA2 and Hero11 mediate similar conformational extension and aggregation suppression of TDP-43
令和6年度(FY2024)2025.01.23Fusion with heat-resistant obscure (Hero) proteins have the potential to improve the molecular property of recombinant proteins