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

Emanuel Peter, Bernhard Dick and Stephan A. Baeurle ()
Additional contact information
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

Nature Communications, 2010, vol. 1, issue 1, 1-7

Abstract: 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.

Date: 2010
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms1121 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:1:y:2010:i:1:d:10.1038_ncomms1121

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms1121

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().