The Fungal Phytochrome FphA from Aspergillus nidulans

The Fungal Phytochrome FphA from Aspergillus nidulans
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DOI:
10.1074/jbc.m805506200
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发表时间:
2008-12-12
影响因子:
4.8
通讯作者:
Frankenberg-Dinkel, Nicole
Frankenberg-Dinkel, Nicole
中科院分区:
生物学2区
文献类型:
--
作者:
Brandt, Sonja;von Stetten, David;Frankenberg-Dinkel, Nicole

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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.