Arabidopsis nph1 and npl1: Blue light receptors that mediate both phototropism and chloroplast relocation
It is demonstrated that npl1, like nph1, noncovalently binds the chromophore flavin mononucleotide (FMN) within two specialized PAS domains, termed LOV domains, indicating that nPL1 also functions as a light receptor kinase.
Phototropin blue-light receptors.
- J. Christie
- Biology, Environmental ScienceAnnual Review of Plant Biology
- 1 May 2007
The photochemical and biochemical events underlying phototropin activation are summarized in addition to the current knowledge of the molecular mechanisms associated with photoreceptor signaling.
Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin.
- M. Salomon, J. Christie, E. Knieb, U. Lempert, W. Briggs
- Biology, ChemistryBiochemistry
- 11 July 2000
It is demonstrated that the LOV domains of Avena sativa phototropin undergo a self-contained photocycle characterized by a loss of blue light absorbance in response to light and a spontaneous recovery of the blue light-absorbing form in the dark.
The Photocycle of a Flavin-binding Domain of the Blue Light Photoreceptor Phototropin*
- T. Swartz, Stephanie B. Corchnoy, R. Bogomolni
- Biology, ChemistryJournal of Biological Chemistry
- 28 September 2001
It has been shown that the metastable species is likely a flavin-cysteine (Cys39 thiol) adduct at the flavin C(4a) position, and Titrations of LOV2 using chromophore fluorescence as an indicator suggest that Cys39 exists as a thiolate.
Phototropins 1 and 2: versatile plant blue-light receptors.
- W. Briggs, J. Christie
- Environmental Science, BiologyTrends in Plant Science
- 1 May 2002
LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide.
- J. Christie, M. Salomon, K. Nozue, M. Wada, W. Briggs
- BiologyProceedings of the National Academy of Sciences…
- 20 July 1999
These findings support the earlier model that nPH1 is a dual-chromophoric flavoprotein photoreceptor regulating phototropic responses in higher plants and propose the name phototropin to designate the nph1 holoprotein.
Plant UVR8 Photoreceptor Senses UV-B by Tryptophan-Mediated Disruption of Cross-Dimer Salt Bridges
- J. Christie, A. Arvai, E. Getzoff
- Biology, ChemistryScience
- 23 March 2012
Donuts Dissociate In Arabidopsis, the UVR8 protein responds to ultraviolet-B (UV-B) light by dissociating into monomers, which are then available to interact with downstream factors that enact the…
Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function.
- J. Christie, T. Swartz, R. Bogomolni, W. Briggs
- Biology, Environmental ScienceThe Plant Journal
- 1 October 2002
Photochemical and biochemical analyses indicate that the LOV1 and LOV2 domains of phot2 exhibit distinct roles, and plays a major role in mediating light-dependent autophosphorylation of full-length phot1 expressed in insect cells and transgenic Arabidopsis.
Arabidopsis NPH1: a flavoprotein with the properties of a photoreceptor for phototropism.
- J. Christie, P. Reymond, W. Briggs
- BiologyScience
- 27 November 1998
The fluorescence excitation spectrum of the recombinant protein is similar to the action spectrum for phototropism, consistent with the conclusion that NPH1 is an autophosphorylating flavoprotein photoreceptor mediating phototropic responses in higher plants.
The photoreversible fluorescent protein iLOV outperforms GFP as a reporter of plant virus infection
- S. Chapman, C. Faulkner, J. Christie
- BiologyProceedings of the National Academy of Sciences
- 16 December 2008
iLOV offers greater utility in FP-tagging of viral gene products and represents a viable alternative where functional protein expression is limited by steric constraints or genome size.
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