Transient Sub-cellular Localization and In Vivo Protein-Protein Interaction Study of Multiple Abiotic Stress-Responsive AteIF4A-III and AtALY4 Proteins in Arabidopsis thaliana
Major abiotic stress factors such as drought, salinity, hypoxia, and extreme temperatures along with rapid global climate change have had a huge negative impact on agricultural productivity. Understanding the abiotic stress-responsive molecular mechanisms and its associated proteins is extremely imp...
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| Published in: | Plant molecular biology reporter Vol. 38; no. 4; pp. 538 - 553 |
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| Main Authors: | , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
New York
Springer US
01.12.2020
Springer Nature B.V |
| Subjects: | |
| ISSN: | 0735-9640, 1572-9818 |
| Online Access: | Get full text |
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| Summary: | Major abiotic stress factors such as drought, salinity, hypoxia, and extreme temperatures along with rapid global climate change have had a huge negative impact on agricultural productivity. Understanding the abiotic stress-responsive molecular mechanisms and its associated proteins is extremely important to advance our knowledge towards developing multiple abiotic stress tolerance in plants. Firstly, basic understanding at transient level would be a vital foundation to accomplish this goal. Therefore, our present study aimed at understanding the sub-cellular localization of Eukaryotic Initiation Factor 4A-III (AteIF4A-III), a key DEAD-box RNA helicase, and Always Early 4 (AtALY4), an mRNA export factor, and their in vivo protein-protein interaction with major abiotic stress–associated proteins under control and multiple abiotic stress conditions. AteIF4A-III and AtALY4 were localized to the nucleus as evident by transient protoplast assay. AteIF4A-III has shown strong interaction with a negative regulator of multiple abiotic stresses, Stress Response Suppressor 1 (AtSTRS1) in Bi-FC assay. Further, the flow cytometry analysis has shown the strong interaction between them. Interestingly, under multiple abiotic stress treatment, the interacting partners were rapidly re-localized from nucleus to cytoplasm and cytoplasmic space. Similar results were observed when N- and C-terminal fusions of AteIF4A-III and AtALY4 treated under multiple abiotic stresses. Our study reveals that AteIF4A-III, AtALY4, and abiotic stress–associated protein AtSTRS1 are among the key proteins associated with multiple abiotic stress responses in plants. |
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| Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| ISSN: | 0735-9640 1572-9818 |
| DOI: | 10.1007/s11105-020-01219-w |