1. In plantavalidation of HK1 homodimerization and recruitment of preferential HPt downstream partners involved in poplar multistep phosphorelay systems
- Author
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M. Miranda, Emilien Foureau, Christiane Depierreux, Gabriella S. Scippa, Lucie Bertheau, Marc Clastre, François Héricourt, Sabine Carpin, Françoise Chefdor, Domenico Morabito, Vincent Courdavault, Nicolas Papon, Franck Brignolas, and L.F. Rojas Hoyos
- Subjects
biology ,Kinase ,fungi ,Plant Science ,biology.organism_classification ,Cytoplasmic part ,Yeast ,Protein–protein interaction ,Interaction studies ,Bimolecular fluorescence complementation ,Biochemistry ,Arabidopsis ,Receptor ,Ecology, Evolution, Behavior and Systematics - Abstract
Multistep phosphorelays involve a phosphate transfer from sensor histidine-aspartate kinases (HKs) to response regulators (RRs), via histidine-containing phosphotransfer proteins (HPts). In Arabidopsis, some AHK receptors are organized as homodimers and able to interact with HPts (AHPs). However, there are no data available concerning the dimerization of the Arabidopsis osmosensor AHK1. Although only AHP2 is able to interact with AHK1 in yeast, validation of this interaction remains to be clarified in planta. The ability of poplar HK1 osmosensor, homologous to AHK1, to homodimerize and interact with three HPts (HPt2, 7 and 9) as preferential partners has been previously shown by yeast two-hybrid assay. However, protein interaction studies need to use complementary approaches to avoid interaction artifacts. Here, we confirmed in planta homodimerization of the cytoplasmic part of HK1 (HK1-CP) and the functional relevance of HK1-CP/HPt interactions by bimolecular fluorescence complementation assays. This wor...
- Published
- 2013