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Shannon M. Harper,
Lori C. Neil,
Kevin H. Gardner*
Abstract:
Phototropins are light-activated kinases important for plantresponses to blue light. Light initiates signaling in theseproteins by generating a covalent protein–flavin mononucleotide(FMN) adduct within sensory Per-ARNT-Sim (PAS) domains. We characterizedthe light-dependent changes of a phototropin PAS domain by solutionnuclear magnetic resonance spectroscopy and found that an helixlocated outside the canonical domain plays a key role in thisactivation process. Although this helix associates with thePAS core in the dark, photoinduced changes in the domain structuredisrupt this interaction. We propose that this mechanism coupleslight-dependent bond formation to kinase activation and identifiesa signaling pathway conserved among PAS domains.
Departments of Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390–9038, USA.
* To whom correspondence should be addressed at Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390–9038, USA. E-mail: kevin.gardner{at}utsouthwestern.edu
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helix located outside the canonical domain plays a key role in this activation process. Although this helix associates with the PAS core in the dark, photoinduced changes in the domain structure disrupt this interaction. We propose that this mechanism couples light-dependent bond formation to kinase activation and identifies a signaling pathway conserved among PAS domains. 
