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

Jessica Colombo, Adrien Antkowiak, Konstantin Kogan, Tommi Kotila, Jenna Elliott, Audrey Guillotin, Pekka Lappalainen and Alphée Michelot ()
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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

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20827-4

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DOI: 10.1038/s41467-020-20827-4

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