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DOE OSTI · 2512408

Transforming an ATP-dependent enzyme into a dissipative, self-assembling system

Li, Yiying [University of California, San Diego, La Jolla, CA (United States)] (ORCID:0000000335666008)·Zhu, Jie [University of California, San Diego, La Jolla, CA (United States)]·Zhang, Zhiyin [University of California, San Diego, La Jolla, CA (United States)]·Wei, Jiapeng [University of Cambridge (United Kingdom)]·Wang, Fengbin [University of Virginia, Charlottesville, VA (United States); University of Alabama, Birmingham, AL (United States)]·Meisl, Georg [University of Cambridge (United Kingdom)] (ORCID:0000000265627715)·Knowles, Tuomas P. J. [University of Cambridge (United Kingdom)] (ORCID:0000000278790140)·Egelman, Edward H. [University of Virginia, Charlottesville, VA (United States)]·Tezcan, F. Akif [University of California, San Diego, La Jolla, CA (United States)] (ORCID:0000000247336500)
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Abstract

Nucleoside triphosphate (NTP)-dependent protein assemblies such as microtubules and actin filaments have inspired the development of diverse chemically fueled molecular machines and active materials but their functional sophistication has yet to be matched by design. Given this challenge, we asked whether it is possible to transform a natural adenosine 5'-triphosphate (ATP)-dependent enzyme into a dissipative self-assembling system, thereby altering the structural and functional mode in which chemical energy is used. Furthermore we report that FtsH (filamentous temperature-sensitive protease H), a hexameric ATPase involved in membrane protein degradation, can be readily engineered to form one-dimensional helical nanotubes. FtsH nanotubes require constant energy input to maintain their integrity and degrade over time with the concomitant hydrolysis of ATP, analogous to natural NTP-dependent cytoskeletal assemblies. Yet, in contrast to natural dissipative systems, ATP hydrolysis is catalyzed by free FtsH protomers and FtsH nanotubes serve to conserve ATP, leading to transient assemblies whose lifetimes can be tuned from days to minutes through the inclusion of external ATPases in solution.

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59 BASIC BIOLOGICAL SCIENCESBiomaterialsProteinsStructural biology

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Li, Yiying [University of California, San Diego, La Jolla, CA (United States)] (ORCID:0000000335666008), Zhu, Jie [University of California, San Diego, La Jolla, CA (United States)], Zhang, Zhiyin [University of California, San Diego, La Jolla, CA (United States)], Wei, Jiapeng [University of Cambridge (United Kingdom)], Wang, Fengbin [University of Virginia, Charlottesville, VA (United States); University of Alabama, Birmingham, AL (United States)], Meisl, Georg [University of Cambridge (United Kingdom)] (ORCID:0000000265627715), Knowles, Tuomas P. J. [University of Cambridge (United Kingdom)] (ORCID:0000000278790140), Egelman, Edward H. [University of Virginia, Charlottesville, VA (United States)], Tezcan, F. Akif [University of California, San Diego, La Jolla, CA (United States)] (ORCID:0000000247336500). 2025-01-13. Transforming an ATP-dependent enzyme into a dissipative, self-assembling system. https://doi.org/10.1038/s41589-024-01811-1

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