Molecular Genetics and Genomics

, Volume 281, Issue 1, pp 35–42 | Cite as

Mapping the interaction sites of Aspergillus nidulans phytochrome FphA with the global regulator VeA and the White Collar protein LreB

  • Janina Purschwitz
  • Sylvia Müller
  • Reinhard Fischer
Original Paper


Aspergillus nidulans senses red and blue-light and employs a phytochrome and a Neurospora crassa White Collar (WC) homologous system for light perception and transmits this information into developmental decisions. Under light conditions it undergoes asexual development and in the dark it develops sexually. The phytochrome FphA consists of a light sensory domain and a signal output domain, consisting of a histidine kinase and a response regulator domain. Previously it was shown that the phytochrome FphA directly interacts with the WC-2 homologue, LreB and another regulator, VeA. In this paper we mapped the interaction of FphA with LreB to the histidine kinase and the response regulator domain at the C-terminus in vivo using the bimolecular fluorescence complementation assay and in vitro by co-immunoprecipitation. In comparison, VeA interacted with FphA only at the histidine kinase domain. We present evidence that VeA occurs as a phosphorylated and a non-phosphorylated form in the cell. The phosphorylation status of the protein was independent of the light receptors FphA, LreB and the WC-1 homologue LreA.


Aspergillus nidulans Phytochrome Red-light response Blue-light response 


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Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  • Janina Purschwitz
    • 1
  • Sylvia Müller
    • 1
  • Reinhard Fischer
    • 1
  1. 1.Institute of Applied Biosciences, Applied MicrobiologyUniversity of Karlsruhe, Karlsruhe Institute of Technology (KIT)KarlsruheGermany

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