4.8 Article

An engineered protein-phosphorylation toggle network with implications for endogenous network discovery

期刊

SCIENCE
卷 373, 期 6550, 页码 -

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AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aav0780

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资金

  1. Siebel Scholars Award
  2. Eni-MIT Energy Research Fellowship
  3. National Science Foundation [DGE1122374, SA5284-11210]
  4. U.S. Army Research Office [W911NF-09-D-0001]
  5. National Institutes of Health [P50 GM098792]

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The research team created a bistable toggle switch in Saccharomyces cerevisiae using a cross-repression topology, and developed a computational framework to search for and validate other large and similar bistable networks. This highlights the potential of building synthetic protein-protein networks.
Synthetic biological networks comprising fast, reversible reactions could enable engineering of new cellular behaviors that are not possible with slower regulation. Here, we created a bistable toggle switch in Saccharomyces cerevisiae using a cross-repression topology comprising 11 protein-protein phosphorylation elements. The toggle is ultrasensitive, can be induced to switch states in seconds, and exhibits long-term bistability. Motivated by our toggle's architecture and size, we developed a computational framework to search endogenous protein pathways for other large and similar bistable networks. Our framework helped us to identify and experimentally verify five formerly unreported endogenous networks that exhibit bistability. Building synthetic protein-protein networks will enable bioengineers to design fast sensing and processing systems, allow sophisticated regulation of cellular processes, and aid discovery of endogenous networks with particular functions.

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