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A functional family of fluorescent nucleotide analogues to investigate actin dynamics and energetics

Author

Listed:
  • Jessica Colombo

    (Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems)

  • Adrien Antkowiak

    (Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems)

  • Konstantin Kogan

    (HiLIFE Institute of Biotechnology)

  • Tommi Kotila

    (HiLIFE Institute of Biotechnology)

  • Jenna Elliott

    (Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems)

  • Audrey Guillotin

    (Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems)

  • Pekka Lappalainen

    (HiLIFE Institute of Biotechnology)

  • Alphée Michelot

    (Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems)

Abstract

Actin polymerization provides force for vital processes of the eukaryotic cell, but our understanding of actin dynamics and energetics remains limited due to the lack of high-quality probes. Most current probes affect dynamics of actin or its interactions with actin-binding proteins (ABPs), and cannot track the bound nucleotide. Here, we identify a family of highly sensitive fluorescent nucleotide analogues structurally compatible with actin. We demonstrate that these fluorescent nucleotides bind to actin, maintain functional interactions with a number of essential ABPs, are hydrolyzed within actin filaments, and provide energy to power actin-based processes. These probes also enable monitoring actin assembly and nucleotide exchange with single-molecule microscopy and fluorescence anisotropy kinetics, therefore providing robust and highly versatile tools to study actin dynamics and functions of ABPs.

Suggested Citation

  • Jessica Colombo & Adrien Antkowiak & Konstantin Kogan & Tommi Kotila & Jenna Elliott & Audrey Guillotin & Pekka Lappalainen & Alphée Michelot, 2021. "A functional family of fluorescent nucleotide analogues to investigate actin dynamics and energetics," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20827-4
    DOI: 10.1038/s41467-020-20827-4
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