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Regulation of ABI5 expression by ABF3 during salt stress responses in Arabidopsis thaliana.


ABSTRACT:

Background

Basic region/leucine zippers (bZIPs) are transcription factors (TFs) encoded by a large gene family in plants. ABF3 and ABI5 are Group A bZIP TFs that are known to be important in abscisic acid (ABA) signaling. However, questions of whether ABF3 regulates ABI5 are still present.

Results

In vitro kinase assay results showed that Thr-128, Ser-134, and Thr-451 of ABF3 are calcium-dependent protein kinase phosphorylation sites. Bimolecular fluorescence complementation (BiFC) analysis results showed a physical interaction between ABF3 and 14-3-3?. A Thr-451 to Ala point mutation abolished the interaction but did not change the subcellular localization. In addition, the Arabidopsis protoplast transactivation assay using a luciferase reporter exhibited ABI5 activation by either ABF3 alone or by co-expression of ABF3 and 14-3-3?. Moreover, chromatin immunoprecipitation-qPCR results showed that in Arabidopsis, ABI5 ABA-responsive element binding proteins (ABREs) of the promoter region (between -?1376 and -?455) were enriched by ABF3 binding under normal and 150 mM NaCl salt stress conditions.

Conclusion

Taken together, our results demonstrated that ABI5 expression is regulated by ABF3, which could contribute to salt stress tolerance in Arabidopsis thaliana.

SUBMITTER: Chang HC 

PROVIDER: S-EPMC6689043 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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Publications

Regulation of ABI5 expression by ABF3 during salt stress responses in Arabidopsis thaliana.

Chang Hui-Chun HC   Tsai Min-Chieh MC   Wu Sih-Sian SS   Chang Ing-Feng IF  

Botanical studies 20190809 1


<h4>Background</h4>Basic region/leucine zippers (bZIPs) are transcription factors (TFs) encoded by a large gene family in plants. ABF3 and ABI5 are Group A bZIP TFs that are known to be important in abscisic acid (ABA) signaling. However, questions of whether ABF3 regulates ABI5 are still present.<h4>Results</h4>In vitro kinase assay results showed that Thr-128, Ser-134, and Thr-451 of ABF3 are calcium-dependent protein kinase phosphorylation sites. Bimolecular fluorescence complementation (BiFC  ...[more]

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