Histone Deacetylase Complex1 Expression Level Titrates Plant Growth and Abscisic Acid Sensitivity in <i>Arabidopsis</i>

Perrella, Giorgio; Lopez-Vernaza, Manuel A.; Carr, Craig; Sani, Emanuela; Gosselé, Veronique; Verduyn, Christoph; Kellermeier, Fabian; Hannah, Matthew A.; Amtmann, Anna

doi:10.1105/tpc.113.114835

Cited by 98 publications

(135 citation statements)

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“…Histone acetylation has been demonstrated to function in different plant hormones (23,(26)(27)(28)(29), and several histone deacetylases are known to be involved in the regulation of gene expression (30)(31)(32)(33)(34)(35)(36)(37). The data presented here showed that the C-terminal domain of EIN2 (EIN2-C) is the key factor that drives alterations in histone acetylation during the ethylene response.…”

Section: Discussionmentioning

confidence: 65%

EIN2 mediates direct regulation of histone acetylation in the ethylene response

Zhang

Wang

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

132

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Ethylene gas is essential for developmental processes and stress responses in plants. Although the membrane-bound protein EIN2 is critical for ethylene signaling, the mechanism by which the ethylene signal is transduced remains largely unknown. Here we show the levels of H3K14Ac and H3K23Ac are correlated with the levels of EIN2 protein and demonstrate EIN2 C terminus (EIN2-C) is sufficient to rescue the levels of H3K14/23Ac of ein2-5 at the target loci, using CRISPR/dCas9-EIN2-C. Chromatin immunoprecipitation followed by deep sequencing (ChIP-seq) and ChIP-reChIP-seq analyses revealed that EIN2-C associates with histone partially through an interaction with EIN2 nuclear-associated protein1 (ENAP1), which preferentially binds to the genome regions that are associated with actively expressed genes both with and without ethylene treatments. Specifically, in the presence of ethylene, ENAP1-binding regions are more accessible upon the interaction with EIN2, and more EIN3 proteins bind to the loci where ENAP1 is enriched for a quick response. Together, these results reveal EIN2-C is the key factor regulating H3K14Ac and H3K23Ac in response to ethylene and uncover a unique mechanism by which ENAP1 interacts with chromatin, potentially preserving the open chromatin regions in the absence of ethylene; in the presence of ethylene, EIN2 interacts with ENAP1, elevating the levels of H3K14Ac and H3K23Ac, promoting more EIN3 binding to the targets shared with ENAP1 and resulting in a rapid transcriptional regulation.T he plant hormone ethylene is essential for a myriad of physiological and developmental processes. It is important in responses to stress, such as drought, cold, flooding, and pathogen infection (1, 2), and modulates stem cell division (3). The common aquatic ancestor of plants possessed the ethylene signaling pathway and the mechanism has been elucidated by analysis of Arabidopsis (4). Ethylene is perceived by a family of receptors bound to the membrane of the endoplasmic reticulum (ER) that are similar in sequence and structure to bacterial two-component histidine kinases (5-9). Each ethylene receptor has an N-terminal transmembrane domain, and the receptors form dimers that bind ethylene via a copper cofactor RAN1 (10, 11). Signaling from one of the receptors, ETR1, induces its physical association with the ER-localized protein RTE1 (12). The ethylene receptors function redundantly to negatively regulate ethylene responses (5) via a downstream Raf-like protein kinase called CTR1 (13,14).In the absence of ethylene, both the ethylene receptors and CTR1 are active, and CTR1 is associated with the ER membrane through a direct interaction with ETR1 (13). The CTR1 downstream factor, EIN2, is localized to the ER membrane, where it interacts with ETR1 (15). The protein stability of EIN2 is regulated by two F-box proteins, ETP1 and ETP2, which mediated its degradation by the ubiquitin-proteasome pathway (16). In the absence of ethylene, the CTR1-mediated phosphorylation at the C-terminal end of EIN2 (EIN2-C) leads to ...

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Section: Discussionmentioning

confidence: 65%

EIN2 mediates direct regulation of histone acetylation in the ethylene response

Zhang

Wang

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

132

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“…In yeast, RPD3, the ortholog of Arabidopsis HDA6, has been shown to be part of a large protein complex that includes transcriptional repressors such as Switch Independent3 and Unscheduled Meiotic gene Expression1 (Grzenda et al, 2009). And there is evidence that plant HDAs also operate in multiprotein complexes containing histone-binding proteins, corepressors, and associated proteins (Gu et al, 2011;Perrella et al, 2013;López-González et al, 2014). It is thus possible that the hda6-8 mutation in the E-R motif affects the interaction of HDA6 with the complex.…”

Section: A Highly Conserved Domain In Hda6 Is Required For Its Targetmentioning

confidence: 99%

HISTONE DEACETYLASE6 Controls Gene Expression Patterning and DNA Methylation-Independent Euchromatic Silencing

et al. 2015

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To investigate the role of chromatin regulators in patterning gene expression, we employed a unique epigenetically controlled and highly tissue-specific green fluorescent protein reporter line in Arabidopsis (Arabidopsis thaliana). Using a combination of forward and reverse genetic approaches on this line, we show here that distinct epigenetic regulators are involved in silencing the transgene in different tissues. The forward genetic screen led to the identification of a novel HISTONE DEACETYLASE6 (HDA6) mutant allele (epigenetic control1, hda6-8). This allele differs from the previously reported alleles, as it did not affect DNA methylation and only had a very modest effect on the release of transposable elements and other heterochromatic transcripts. Overall, our data shows that HDA6 has at least two clearly separable activities in different genomic regions. In addition, we present an unexpected role for HDA6 in the control of DNA methylation at CG dinucleotides.

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“…Including an additionally expressed red fluorescent protein from this T-DNA, the system allows the application of a ratiometric bimolecular fluorescence complementation (rBiFC) assay, significantly enhancing the credibility of results compared with classical split-FP-based vector systems (Grefen and Blatt, 2012). This system has since been successfully employed to analyze interactions of a range of different proteins (Karnik et al, 2013bPerrella et al, 2013;Hachez et al, 2014;Lipka et al, 2014.…”

mentioning

confidence: 99%

Binary 2in1 Vectors Improve in Planta (Co)localization and Dynamic Protein Interaction Studies

Hecker

Wallmeroth²,

Peter³

et al. 2015

Plant Physiol.

100

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Fluorescence-based protein-protein interaction techniques are vital tools for understanding in vivo cellular functions on a mechanistic level. However, only under the condition of highly efficient (co)transformation and accumulation can techniques such as Förster resonance energy transfer (FRET) realize their potential for providing highly accurate and quantitative interaction data. FRET as a fluorescence-based method unifies several advantages, such as measuring in an in vivo environment, real-time context, and the ability to include transient interactions as well as detecting the mere proximity of proteins. Here, we introduce a novel vector set that incorporates the benefit of the recombination-based 2in1 cloning system with the latest state-of-the-art fluorescent proteins for optimal coaccumulation and FRET output studies. We demonstrate its utility across a range of methods. Merging the 2in1 cloning system with new-generation FRET fluorophore pairs allows for enhanced detection, speeds up the preparation of clones, and enables colocalization studies and the identification of meaningful protein-protein interactions in vivo.Two technological advances allowed the field of modern cell biology to emerge: the development of high-resolution microscopes and the groundbreaking work in the development of fluorescent proteins (FPs) that were originally isolated from jellyfish (for review, see Day and Davidson, 2009;Zimmer, 2009). Genetically encoded FPs can be fused directly to proteins of choice, offering insights into their functional properties by allowing researchers to monitor subcellular localization, chemical environment, interaction, movement, and/or turnover rate.Research on the FPs themselves has exploded in the past two decades, and a range of technological improvements to and variations of the FPs were generated. These improvements include novel spectral properties from all areas of the color palette and from a diverse range of organisms. They also extend to a multitude of parameters, such as brightness, folding efficiency, chromophore oxidation rate, quantum yield, pH, and photostability (Day and Davidson, 2009). Taken together, these optimizations further the possibilities of available methods or prompt the development of new techniques.In 1946, the German scientist Theodor Förster laid the theoretical foundation for resonance energy transfer, now known as Förster resonance energy transfer (FRET;Forster, 1946). According to this theory, a donor chromophore in an excited state can transfer the excitation energy to a nearby acceptor chromophore via dipole-dipole coupling without the emission of a photon (for review, see Clegg, 2009;Ishikawa-Ankerhold et al., 2012). FRET depends on the spectral overlap between the emission spectrum of the donor and the absorbance spectrum of the acceptor chromophores. It also depends on the fluorescence quantum yield and the excited state lifetime of the donor in the absence of an acceptor as well as the relative orientation of the two chromophores. Most importantly, FRET ef...

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Histone Deacetylase Complex1 Expression Level Titrates Plant Growth and Abscisic Acid Sensitivity in Arabidopsis

Cited by 98 publications

References 57 publications

EIN2 mediates direct regulation of histone acetylation in the ethylene response

EIN2 mediates direct regulation of histone acetylation in the ethylene response

HISTONE DEACETYLASE6 Controls Gene Expression Patterning and DNA Methylation-Independent Euchromatic Silencing

Binary 2in1 Vectors Improve in Planta (Co)localization and Dynamic Protein Interaction Studies

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