Evidence for weak interaction between phytochromes Agp1 and Agp2 from Agrobacterium fabrum

Evidence for weak interaction between phytochromes Agp1 and Agp2 from Agrobacterium fabrum

During bacterial conjugation, plasmid DNA is transferred from cell to cell. In Agrobacterium fabrum, conjugation is regulated by the phytochrome photoreceptors Agp1 and Agp2. Both contribute equally to this regulation. Agp1 and Agp2 are histidine kinases, but, for Agp2, we found no autophosphorylati...

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Bibliographic Details
Published in:FEBS letters Vol. 593; no. 9; pp. 926 - 941
Main Authors: Xue, Peng, El Kurdi, Afaf, Kohler, Anja, Ma, Hongju, Kaeser, Gero, Ali, Arin, Fischer, Reinhard, Krauß, Norbert, Lamparter, Tilman
Format: Journal Article
Language:English
Published: England 01-05-2019
Subjects:
Agrobacterium - metabolism
Agrobacterium fabrum
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
biliverdin
histidine kinase
Histidine Kinase - metabolism
Mutation
phosphorylation
Phosphorylation - genetics
phytochrome
Phytochrome - genetics
Phytochrome - metabolism
Protein Binding
protein interaction
phytochrome
histidine kinase
protein interaction
phosphorylation
biliverdin
Agrobacterium fabrum
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Summary:During bacterial conjugation, plasmid DNA is transferred from cell to cell. In Agrobacterium fabrum, conjugation is regulated by the phytochrome photoreceptors Agp1 and Agp2. Both contribute equally to this regulation. Agp1 and Agp2 are histidine kinases, but, for Agp2, we found no autophosphorylation activity. A clear autophosphorylation signal, however, was obtained with mutants in which the phosphoaccepting Asp of the C‐terminal response regulator domain is replaced. Thus, the Agp2 histidine kinase differs from the classical transphosphorylation pattern. We performed size exclusion, photoconversion, dark reversion, autophosphorylation, chromophore assembly kinetics and fluorescence resonance energy transfer measurements on mixed Agp1/Agp2 samples. These assays pointed to an interaction between both proteins. This could partially explain the coaction of both phytochromes in the cell.
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ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.13376