The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1
IntroductionThe Arabidopsis abc1k1/pgr6 (Activity of BC1 complex/proton regulation 6) mutant is characterized by photosynthetic and conditional developmental phenotypes triggered by stressful red as well as high light. The Arabidopsis ABC1-like kinases belong to the atypical kinase family and contai...
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| Format: | Article |
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Frontiers Media S.A.
2024-11-01
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| Series: | Frontiers in Plant Science |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fpls.2024.1491719/full |
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| author | Maud Turquand Ana Rita Justo Da Silva Thibaut Pralon Fiamma Longoni Felix Kessler Joy Collombat |
| author_facet | Maud Turquand Ana Rita Justo Da Silva Thibaut Pralon Fiamma Longoni Felix Kessler Joy Collombat |
| author_sort | Maud Turquand |
| collection | DOAJ |
| description | IntroductionThe Arabidopsis abc1k1/pgr6 (Activity of BC1 complex/proton regulation 6) mutant is characterized by photosynthetic and conditional developmental phenotypes triggered by stressful red as well as high light. The Arabidopsis ABC1-like kinases belong to the atypical kinase family and contain conserved ATP-binding and hydrolysis motifs, but their physiological requirement has never been investigated.MethodsBy mutation to asparagine, we demonstrate that the highly conserved active site aspartate residue within ATP-binding motif VIIb is required for the physiological functions of ABC1K1.ResultsComplementation of the abc1k1 knock out mutant with ABC1K1 D400N, failed to restore the wildtype phenotype.DiscussionThese results provide in vivo evidence for a critical role of the active site aspartate residue (D400) of ABC1K1. |
| format | Article |
| id | doaj-art-a8e06c771206420ca143f7fe96f60fbd |
| institution | Kabale University |
| issn | 1664-462X |
| language | English |
| publishDate | 2024-11-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj-art-a8e06c771206420ca143f7fe96f60fbd2024-11-19T14:30:10ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2024-11-011510.3389/fpls.2024.14917191491719The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1Maud Turquand0Ana Rita Justo Da Silva1Thibaut Pralon2Fiamma Longoni3Felix Kessler4Joy Collombat5Plant Physiology Laboratory, Institute of Biology, Université de Neuchâtel, Neuchâtel, SwitzerlandPlant Physiology Laboratory, Institute of Biology, Université de Neuchâtel, Neuchâtel, SwitzerlandCDC-LAB, Plan-les-Ouates, SwitzerlandPlant Physiology Laboratory, Institute of Biology, Université de Neuchâtel, Neuchâtel, SwitzerlandPlant Physiology Laboratory, Institute of Biology, Université de Neuchâtel, Neuchâtel, SwitzerlandPlant Physiology Laboratory, Institute of Biology, Université de Neuchâtel, Neuchâtel, SwitzerlandIntroductionThe Arabidopsis abc1k1/pgr6 (Activity of BC1 complex/proton regulation 6) mutant is characterized by photosynthetic and conditional developmental phenotypes triggered by stressful red as well as high light. The Arabidopsis ABC1-like kinases belong to the atypical kinase family and contain conserved ATP-binding and hydrolysis motifs, but their physiological requirement has never been investigated.MethodsBy mutation to asparagine, we demonstrate that the highly conserved active site aspartate residue within ATP-binding motif VIIb is required for the physiological functions of ABC1K1.ResultsComplementation of the abc1k1 knock out mutant with ABC1K1 D400N, failed to restore the wildtype phenotype.DiscussionThese results provide in vivo evidence for a critical role of the active site aspartate residue (D400) of ABC1K1.https://www.frontiersin.org/articles/10.3389/fpls.2024.1491719/fullchloroplastatypical kinase ABC1K1photosynthesisactive site mutationcomplementation |
| spellingShingle | Maud Turquand Ana Rita Justo Da Silva Thibaut Pralon Fiamma Longoni Felix Kessler Joy Collombat The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1 Frontiers in Plant Science chloroplast atypical kinase ABC1K1 photosynthesis active site mutation complementation |
| title | The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1 |
| title_full | The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1 |
| title_fullStr | The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1 |
| title_full_unstemmed | The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1 |
| title_short | The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1 |
| title_sort | conserved active site aspartate residue is required for the function of the chloroplast atypical kinase abc1k1 |
| topic | chloroplast atypical kinase ABC1K1 photosynthesis active site mutation complementation |
| url | https://www.frontiersin.org/articles/10.3389/fpls.2024.1491719/full |
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