Abscisic acid-responsive element binding transcription factors contribute to proline synthesis and stress adaptation in Arabidopsis

2021 ◽  
Vol 261 ◽  
pp. 153414
Author(s):  
Asis Shrestha ◽  
Daniel Kingsley Cudjoe ◽  
Mohammad Kamruzzaman ◽  
Shahid Siddique ◽  
Fabio Fiorani ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Abscisic Acid ◽  
Stress Adaptation ◽  
Abscisic Acid Responsive Element ◽  
Responsive Element

Involvement of WRKY Transcription Factors in Abscisic-Acid-Induced Cold Tolerance of Banana Fruit

2017 ◽  
Vol 65 (18) ◽  
pp. 3627-3635 ◽  
Author(s):  
Dong-lan Luo ◽  
Liang-jie Ba ◽  
Wei Shan ◽  
Jian-fei Kuang ◽  
Wang-jin Lu ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Abscisic Acid ◽  
Cold Tolerance ◽  
Banana Fruit ◽  
Wrky Transcription Factors

Identification of two independent nucleosome-binding domains in the transcriptional co-activator SPBP

2012 ◽  
Vol 442 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Sagar Darvekar ◽  
Sylvia Sagen Johnsen ◽  
Agnete Bratsberg Eriksen ◽  
Terje Johansen ◽  
Eva Sjøttem
Keyword(s):  
Transcription Factors ◽  
Dependent Manner ◽  
Chromatin Binding ◽  
Binding Region ◽  
Interaction Domain ◽  
Binding Domains ◽  
Element Binding Protein ◽  
Inducible Protein ◽  
Responsive Element ◽  
Nucleosome Binding

Transcriptional regulation requires co-ordinated action of transcription factors, co-activator complexes and general transcription factors to access specific loci in the dense chromatin structure. In the present study we demonstrate that the transcriptional co-regulator SPBP [stromelysin-1 PDGF (platelet-derived growth factor)-responsive element binding protein] contains two independent chromatin-binding domains, the SPBP-(1551–1666) region and the C-terminal extended PHD [ePHD/ADD (extended plant homeodomain/ATRX-DNMT3-DNMT3L)] domain. The region 1551–1666 is a novel core nucleosome-interaction domain located adjacent to the AT-hook motif in the DNA-binding domain. This novel nucleosome-binding region is critically important for proper localization of SPBP in the cell nucleus. The ePHD/ADD domain associates with nucleosomes in a histone tail-dependent manner, and has significant impact on the dynamic interaction between SPBP and chromatin. Furthermore, SPBP and its homologue RAI1 (retinoic-acid-inducible protein 1), are strongly enriched on chromatin in interphase HeLa cells, and both proteins display low nuclear mobility. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP-(1551–1666) and an ePHD/ADD domain with ability to bind nucleosomes. These results indicate that the transcriptional co-regulator SPBP and its homologue RAI1 implicated in Smith–Magenis syndrome and Potocki–Lupski syndrome both belong to the expanding family of chromatin-binding proteins containing several domains involved in specific chromatin interactions.

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