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Open AccessArticle

Functional Divergence of Poplar Histidine-Aspartate Kinase HK1 Paralogs in Response to Osmotic Stress

1
Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC), Université d’Orléans, INRA, USC1328, 45067 Orléans, France
2
Biomolécules et Biotechnologies Végétales (BBV), EA 2106, Université François Rabelais de Tours, 31 avenue Monge, 37200 Tours, France
3
Centre de Biophysique Moléculaire (CBM), CNRS, 45071 Orléans, France
4
Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Jianhua Zhu
Int. J. Mol. Sci. 2016, 17(12), 2061; https://doi.org/10.3390/ijms17122061
Received: 7 October 2016 / Revised: 1 December 2016 / Accepted: 3 December 2016 / Published: 8 December 2016
(This article belongs to the Section Molecular Plant Sciences)
Previous works have shown the existence of protein partnerships belonging to a MultiStep Phosphorelay (MSP) in Populus putatively involved in osmosensing. This study is focused on the identification of a histidine-aspartate kinase, HK1b, paralog of HK1a. The characterization of HK1b showed its ability to homo- and hetero-dimerize and to interact with a few Histidine-containing Phosphotransfer (HPt) proteins, suggesting a preferential partnership in poplar MSP linked to drought perception. Furthermore, determinants for interaction specificity between HK1a/1b and HPts were studied by mutagenesis analysis, identifying amino acids involved in this specificity. The HK1b expression analysis in different poplar organs revealed its co-expression with three HPts, reinforcing the hypothesis of partnership participation in the MSP in planta. Moreover, HK1b was shown to act as an osmosensor with kinase activity in a functional complementation assay of an osmosensor deficient yeast strain. These results revealed that HK1b showed a different behaviour for canonical phosphorylation of histidine and aspartate residues. These phosphorylation modularities of canonical amino acids could explain the improved osmosensor performances observed in yeast. As conserved duplicates reflect the selective pressures imposed by the environmental requirements on the species, our results emphasize the importance of HK1 gene duplication in poplar adaptation to drought stress. View Full-Text
Keywords: histidine-aspartate kinase (HK); histidine-containing phosphotransfer protein (HPt); multistep phosphorelay (MSP); osmosensing; Populus; drought signaling histidine-aspartate kinase (HK); histidine-containing phosphotransfer protein (HPt); multistep phosphorelay (MSP); osmosensing; Populus; drought signaling
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MDPI and ACS Style

Héricourt, F.; Chefdor, F.; Djeghdir, I.; Larcher, M.; Lafontaine, F.; Courdavault, V.; Auguin, D.; Coste, F.; Depierreux, C.; Tanigawa, M.; Maeda, T.; Glévarec, G.; Carpin, S. Functional Divergence of Poplar Histidine-Aspartate Kinase HK1 Paralogs in Response to Osmotic Stress. Int. J. Mol. Sci. 2016, 17, 2061. https://doi.org/10.3390/ijms17122061

AMA Style

Héricourt F, Chefdor F, Djeghdir I, Larcher M, Lafontaine F, Courdavault V, Auguin D, Coste F, Depierreux C, Tanigawa M, Maeda T, Glévarec G, Carpin S. Functional Divergence of Poplar Histidine-Aspartate Kinase HK1 Paralogs in Response to Osmotic Stress. International Journal of Molecular Sciences. 2016; 17(12):2061. https://doi.org/10.3390/ijms17122061

Chicago/Turabian Style

Héricourt, François; Chefdor, Françoise; Djeghdir, Inès; Larcher, Mélanie; Lafontaine, Florent; Courdavault, Vincent; Auguin, Daniel; Coste, Franck; Depierreux, Christiane; Tanigawa, Mirai; Maeda, Tatsuya; Glévarec, Gaëlle; Carpin, Sabine. 2016. "Functional Divergence of Poplar Histidine-Aspartate Kinase HK1 Paralogs in Response to Osmotic Stress" Int. J. Mol. Sci. 17, no. 12: 2061. https://doi.org/10.3390/ijms17122061

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