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The Fungal Phytochrome FphA from Aspergillus nidulans
Citation key ISI:000261469100015
Author Brandt, Sonja and von Stetten, David and G�nther, Mina and Hildebrandt, Peter and Frankenberg-Dinkel, Nicole
Pages 34605-34614
Year 2008
ISSN 0021-9258
DOI 10.1074/jbc.M805506200
Address 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
Journal J. Biol. Chem.
Volume 283
Number 50
Month DEC 12
Abstract The red light-sensing photoreceptor FphA from Aspergillus nidulans is involved in the regulation of developmental processes in response to light. Here we present extended biochemical and spectroscopic characterization of recombinant FphA using a synthetic gene with host-adapted codon usage. The recombinant photosensory domain FphAN753 was shown to display all features of a bona fide phytochrome. It covalently binds biliverdin as chromophore and undergoes red/far-red light-inducible photoconversion with both parent states being protonated. The large N-terminal variable extension of FphA exerts a stabilizing effect on the active Pfr state. Upon substitution of the highly conserved histidine 504, involved in the hydrogen-bonding network of the protein moiety and the chromophore, chromophore attachment and photoreversibility were completely impaired. FphA is a functional sensor histidine kinase with a strong red-light-dependent autophosphorylation activity. Furthermore, intermolecular trans-phosphorylation to the response regulator domain of a second monomer could be demonstrated. Interestingly, co-incubation of FphA and FphA variants led to enhanced autophosphorylation, including the ``inactive'' Pr form. The latter observed phenomenon might suggest that auto- and trans-phosphorylation activity is modulated by additional interaction partners leading to variable phosphorylation events that trigger a specific output response.
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