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Mechanism of signal transduction of the LOV2-Jα photosensor from Avena sativa

Author

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  • Emanuel Peter

    (Institute of Physical and Theoretical Chemistry, University of Regensburg)

  • Bernhard Dick

    (Institute of Physical and Theoretical Chemistry, University of Regensburg)

  • Stephan A. Baeurle

    (Institute of Physical and Theoretical Chemistry, University of Regensburg)

Abstract

Fusion proteins containing blue-light-activable protein domains possess great potential as molecular switches in cell signalling. This has recently been impressively demonstrated by connecting the light oxygen voltage LOV2-Jα-protein domain of A. sativa (AsLOV2-Jα) with the Rac1-GTPase, responsible for regulating the morphology and motility of metazoan cells. However, a target-oriented development of fusion proteins in conjunction with this photosensor is still very challenging, because a detailed understanding of its signal transduction pathway on a molecular level is still lacking. Here, we show through molecular dynamics simulation that, after formation of the cysteinyl-flavin mononucleotide (FMN) adduct, the signalling pathway begins with a rotational reorientation of the residue glutamine 1029 adjacent to the FMN chromophore, transmitting stress through the Iβ strand towards the LOV2-Jα interface. This then results in the breakage of two H-bonds, namely, glutamic acid 1034–Gln995 and aspartic acid (Asp) 1056–Gln1013, at opposite sides of the interface between the Jα helix and the LOV2 domain, ultimately leading to a disruption of Jα helix from the LOV2 core.

Suggested Citation

  • Emanuel Peter & Bernhard Dick & Stephan A. Baeurle, 2010. "Mechanism of signal transduction of the LOV2-Jα photosensor from Avena sativa," Nature Communications, Nature, vol. 1(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:1:y:2010:i:1:d:10.1038_ncomms1121
    DOI: 10.1038/ncomms1121
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