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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Vydáno v:	Plant molecular biology reporter Ročník 38; číslo 4; s. 538 - 553
Hlavní autoři:	Baruah, Indrani, Baruah, Geetanjali, Sahu, Jagajjit, Singha, Dhanawantari L., Dekaboruah, Hariprasanna, Velmurugan, Natarajan, Chikkaputtaiah, Channakeshavaiah
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	New York Springer US 01.12.2020 Springer Nature B.V
Témata:	Abiotic factors Abiotic stress Agricultural production agricultural productivity Arabidopsis thaliana Bioinformatics Biomedical and Life Sciences Climate change Cytoplasm DEAD-box RNA helicases DNA helicase Drought Flow cytometry Global climate Hypoxia In vivo methods and tests Life Sciences Localization Metabolomics molecular biology Molecular modelling mRNA Nuclei (cytology) Original Paper Plant Breeding/Biotechnology Plant Sciences Protein interaction protein-protein interactions Proteins Proteomics protoplasts RNA helicase RNA transport salinity stress response stress tolerance Stresses Strong interactions (field theory) DEAD-box RNA helicases Re-localization Protein-protein interaction AtALY4 Multiple abiotic stresses AteIF4A-III
ISSN:	0735-9640, 1572-9818
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Abstract	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.
AbstractList	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.
Author	Sahu, Jagajjit Baruah, Indrani Chikkaputtaiah, Channakeshavaiah Singha, Dhanawantari L. Dekaboruah, Hariprasanna Baruah, Geetanjali Velmurugan, Natarajan
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Keywords	DEAD-box RNA helicases Re-localization Protein-protein interaction AtALY4 Multiple abiotic stresses AteIF4A-III
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Snippet	Major abiotic stress factors such as drought, salinity, hypoxia, and extreme temperatures along with rapid global climate change have had a huge negative...
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SubjectTerms	Abiotic factors Abiotic stress Agricultural production agricultural productivity Arabidopsis thaliana Bioinformatics Biomedical and Life Sciences Climate change Cytoplasm DEAD-box RNA helicases DNA helicase Drought Flow cytometry Global climate Hypoxia In vivo methods and tests Life Sciences Localization Metabolomics molecular biology Molecular modelling mRNA Nuclei (cytology) Original Paper Plant Breeding/Biotechnology Plant Sciences Protein interaction protein-protein interactions Proteins Proteomics protoplasts RNA helicase RNA transport salinity stress response stress tolerance Stresses Strong interactions (field theory)
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Title	Transient Sub-cellular Localization and In Vivo Protein-Protein Interaction Study of Multiple Abiotic Stress-Responsive AteIF4A-III and AtALY4 Proteins in Arabidopsis thaliana
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