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DC Field | Value | Language |
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dc.contributor.author | Jonwal, Sarvesh | - |
dc.contributor.author | Verma, Neetu | - |
dc.contributor.author | Sinha, Alok Krishna | - |
dc.date.accessioned | 2022-05-31T10:34:32Z | - |
dc.date.available | 2022-05-31T10:34:32Z | - |
dc.date.issued | 2022 | - |
dc.identifier.citation | Plant Science, 321: 111312 | en_US |
dc.identifier.issn | 0168-9452 | - |
dc.identifier.other | https://doi.org/10.1016/j.plantsci.2022.111312 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/abs/pii/S0168945222001364 | - |
dc.identifier.uri | http://223.31.159.10:8080/jspui/handle/123456789/1340 | - |
dc.description | Accepted date: 4 May 2022 | en_US |
dc.description.abstract | The regulation of photosynthesis occurs at different levels including the control of nuclear and plastid genes transcription, RNA processing and translation, protein translocation, assemblies and their post translational modifications. Out of all these, post translational modification enables rapid response of plants towards changing environmental conditions. Among all post-translational modifications, reversible phosphorylation is known to play a crucial role in the regulation of light reaction of photosynthesis. Although, phosphorylation of PS II subunits has been extensively studied but not much attention is given to other photosynthetic complexes such as PS I, Cytochrome b6f complex and ATP synthase. Phosphorylation reaction is known to protect photosynthetic apparatus in challenging environment conditions such as high light, elevated temperature, high salinity and drought. Recent studies have explored the role of photosynthetic protein phosphorylation in conferring plant immunity against the rice blast disease. The evolution of phosphorylation of different subunits of photosynthetic proteins occurred along with the evolution of plant lineage for their better adaptation to the changing environment conditions. In this review, we summarize the progress made in the research field of phosphorylation of photosynthetic proteins and highlights the missing links that need immediate attention. | en_US |
dc.description.sponsorship | The work is supported from the core grant of National Institute of Plant Genome Research from the Department of Biotechnology, Government of India. SJ thanks Department of Biotechnology, Government of India for fellowship. NV Thanks DBT-Biocare Women Scientist Fellowship from Department of Biotechnology, Government of India. AKS thanks Sir J.C. Bose fellowship from Science and Engineering Research Board, Government of India. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Elsevier B.V. | en_US |
dc.subject | Photosynthesis | en_US |
dc.subject | Light reaction | en_US |
dc.subject | Phosphorylation | en_US |
dc.subject | PSI | en_US |
dc.subject | PSII | en_US |
dc.subject | LHCII | en_US |
dc.subject | Photoinhibition | en_US |
dc.title | Regulation of photosynthetic light reaction proteins via reversible phosphorylation | en_US |
dc.type | Article | en_US |
Appears in Collections: | Institutional Publications |
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Sinha AK_2022_3.pdf Restricted Access | 2.23 MB | Adobe PDF | View/Open Request a copy |
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