Modulating mechanical stability of heterodimerization between engineered orthogonal helical domains

Miao Yu, Zhihai Zhao, Zibo Chen, Shimin Le () and Jie Yan ()
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Miao Yu: National University of Singapore
Zhihai Zhao: National University of Singapore
Zibo Chen: University of Washington
Shimin Le: National University of Singapore
Jie Yan: National University of Singapore

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract Mechanically stable specific heterodimerization between small protein domains have a wide scope of applications, from using as a molecular anchorage in single-molecule force spectroscopy studies of protein mechanics, to serving as force-bearing protein linker for modulation of mechanotransduction of cells, and potentially acting as a molecular crosslinker for functional materials. Here, we explore the possibility to develop heterodimerization system with a range of mechanical stability from a set of recently engineered helix-heterotetramers whose mechanical properties have yet to be characterized. We demonstrate this possibility using two randomly chosen helix-heterotetramers, showing that their mechanical properties can be modulated by changing the stretching geometry and the number of interacting helices. These helix-heterotetramers and their derivatives are sufficiently stable over physiological temperature range. Using it as mechanically stable anchorage, we demonstrate the applications in single-molecule manipulation studies of the temperature dependent unfolding and refolding of a titin immunoglobulin domain and α-actinin spectrin repeats.

Date: 2020
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DOI: 10.1038/s41467-020-18323-w

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