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DC Field | Value | Language |
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dc.contributor.author | Ghosh, Shraboni | - |
dc.contributor.author | Kamble, Nitin Uttam | - |
dc.contributor.author | Majee, Manoj | - |
dc.date.accessioned | 2020-09-21T09:58:56Z | - |
dc.date.available | 2020-09-21T09:58:56Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Environmental and Experimental Botany, 180: 104266 | en_US |
dc.identifier.issn | 0098-8472 | - |
dc.identifier.other | https://doi.org/10.1016/j.envexpbot.2020.104266 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0098847220302926 | - |
dc.identifier.uri | http://223.31.159.10:8080/jspui/handle/123456789/1097 | - |
dc.description | Accepted date: 2 September 2020 | en_US |
dc.description.abstract | Saline conditions can significantly affect plant growth and development, leading to massive reduction in crop yield. Herein, we show that a protein repairing enzyme PROTEIN L-ISOASPARTYL METHYLTRANSFERASE imparts salinity stress tolerance in Arabidopsis thaliana by repairing deleterious isoAsp accumulation during salinity stress. We demonstrate that salinity stress accelerates isoAsp accumulation in proteins and also induces PIMT activity in Arabidopsis. Transcript analysis indicates that both PIMT1 and PIMT2 are upregulated in response to salinity stress. Subsequent functional analysis reveals that PIMT1 and PIMT2 overexpression lines are tolerant, while RNAi lines are hyper sensitive to salinity stress in comparison to wild type (WT). Biochemical analyses of thesePIMT transgenic lines also reveals that compromised salinity tolerance of RNAi lines are linked to increased isoAsp accumulation, while improved tolerance of overexpression lines is associated with reduced isoAsp accumulation in proteins. Histochemical and biochemical studies further confirm lower accumulation of ROS and reduced lipid peroxidation in PIMT overexpression lines, while increased ROS accumulation and increased lipid peroxidation in RNAi lines as compared to WT under salinity stress. Interestingly, PIMToverexpression lines exhibit improved antioxidant enzyme efficiency, while RNAi lines display compromised antioxidant enzyme efficacy as compared to WT type plants. Our study suggests that PIMT improves salinity stress tolerance by restricting salt induced-excess ROS accumulation possibly by repairing isoAsp mediated protein damage of antioxidant enzymes. Our study can be utilized for enhancing salinity stress tolerance of economically important crops. | en_US |
dc.description.sponsorship | This work was supported by a grant from Department of Biotechnology (BT/PR8000/BRB/10/1210/2013), Government of India and core grant of National Institute of Plant Genome Research, New Delhi, India. SG and NUK thank University Grant Commission, Government of India and NIPGR, for research fellowship. We thank technicians of NIPGR central instrumentation facility. We thank Metabolomics facility at NIPGR for ICP-MS analysis (BT/INF/22/SP28268/2018). The authors are thankful to DBT-eLibrary Consortium (DeLCON) for providing access to e-resources. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Elsevier B.V. | en_US |
dc.subject | Salinity stress tolerance | en_US |
dc.subject | PIMT | en_US |
dc.subject | isoAsp | en_US |
dc.subject | ROS | en_US |
dc.subject | Antioxidant enzymes | en_US |
dc.subject | Arabidopsis | en_US |
dc.title | A protein repairing enzyme, PROTEIN L- ISOASPARTYL METHYLTRANSFERASE is involved in salinity stress tolerance by increasing efficiency of ROS-scavenging enzymes | en_US |
dc.type | Article | en_US |
Appears in Collections: | Institutional Publications |
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Majee M_2020_3.pdf Restricted Access | 6.01 MB | Adobe PDF | View/Open Request a copy |
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