دورية أكاديمية
Searching for Osmosensing Determinants in Poplar Histidine-Aspartate Kinases
| العنوان: | Searching for Osmosensing Determinants in Poplar Histidine-Aspartate Kinases |
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| المؤلفون: | Hanae Makhokh, Pierre Lafite, Mélanie Larcher, Frédéric Lamblin, Françoise Chefdor, Christiane Depierreux, Mirai Tanigawa, Tatsuya Maeda, Sabine Carpin, François Héricourt |
| المصدر: | International Journal of Molecular Sciences, Vol 24, Iss 7, p 6318 (2023) |
| بيانات النشر: | MDPI AG, 2023. |
| سنة النشر: | 2023 |
| المجموعة: | LCC:Biology (General) LCC:Chemistry |
| مصطلحات موضوعية: | histidine-aspartate kinase (HK), cache domain, extracellular domain (ECD), transmembrane (TM) domain, MultiStep Phosphorelay (MSP), Osmosensing, Biology (General), QH301-705.5, Chemistry, QD1-999 |
| الوصف: | Previous works have shown the existence of protein partnership, belonging to a MultiStep Phosphorelay (MSP), potentially involved in osmosensing in Populus. The first actor of this signalling pathway belongs to the histidine-aspartate kinase (HK) family, which also includes the yeast osmosensor Sln1, as well as the Arabidopsis putative osmosensor AHK1. In poplar, the homologous AHK1 protein corresponds to a pair of paralogous proteins, HK1a and HK1b, exhibiting an extracellular domain (ECD), as in Sln1 and AHK1. An ECD alignment of AHK1-like proteins, from different plant species, showed a particularly well conserved ECD and revealed the presence of a cache domain. This level of conservation suggested a functional role of this domain in osmosensing. Thus, we tested this possibility by modelling assisted mutational analysis of the cache domain of the Populus HK1 proteins. The mutants were assessed for their ability to respond to different osmotic stress and the results point to an involvement of this domain in HK1 functionality. Furthermore, since HK1b was shown to respond better to stress than HK1a, these two receptors constituted a good system to search for osmosensing determinants responsible for this difference in efficiency. With domain swapping experiments, we finally demonstrated that the cache domain, as well as the second transmembrane domain, are involved in the osmosensing efficiency of these receptors. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 1422-0067 1661-6596 |
| Relation: | https://www.mdpi.com/1422-0067/24/7/6318; https://doaj.org/toc/1661-6596; https://doaj.org/toc/1422-0067 |
| DOI: | 10.3390/ijms24076318 |
| URL الوصول: | https://doaj.org/article/2c6546c44ac744f090b5f6641f67aac0 |
| رقم الأكسشن: | edsdoj.2c6546c44ac744f090b5f6641f67aac0 |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 14220067 16616596 |
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| DOI: | 10.3390/ijms24076318 |