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Twister ribozymes as highly versatile expression platforms for artificial riboswitches

Author

Listed:
  • Michele Felletti

    (University of Konstanz
    Konstanz Research School Chemical Biology (Kors-CB), University of Konstanz)

  • Julia Stifel

    (University of Konstanz
    Konstanz Research School Chemical Biology (Kors-CB), University of Konstanz)

  • Lena A. Wurmthaler

    (University of Konstanz
    Konstanz Research School Chemical Biology (Kors-CB), University of Konstanz)

  • Sophie Geiger

    (University of Konstanz)

  • Jörg S. Hartig

    (University of Konstanz
    Konstanz Research School Chemical Biology (Kors-CB), University of Konstanz)

Abstract

The utilization of ribozyme-based synthetic switches in biotechnology has many advantages such as an increased robustness due to in cis regulation, small coding space and a high degree of modularity. The report of small endonucleolytic twister ribozymes provides new opportunities for the development of advanced tools for engineering synthetic genetic switches. Here we show that the twister ribozyme is distinguished as an outstandingly flexible expression platform, which in conjugation with three different aptamer domains, enables the construction of many different one- and two-input regulators of gene expression in both bacteria and yeast. Besides important implications in biotechnology and synthetic biology, the observed versatility in artificial genetic control set-ups hints at possible natural roles of this widespread ribozyme class.

Suggested Citation

  • Michele Felletti & Julia Stifel & Lena A. Wurmthaler & Sophie Geiger & Jörg S. Hartig, 2016. "Twister ribozymes as highly versatile expression platforms for artificial riboswitches," Nature Communications, Nature, vol. 7(1), pages 1-8, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12834
    DOI: 10.1038/ncomms12834
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    Cited by:

    1. Yuanli Gao & Lei Wang & Baojun Wang, 2023. "Customizing cellular signal processing by synthetic multi-level regulatory circuits," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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