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| 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 |
| Publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 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. |
| Bibtex Type of Publication | Article |
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