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  • EIN2-dependent regulation of acetylation of histone H3K14 and non-canonical histone H3K23 in ethylene signalling.

EIN2-dependent regulation of acetylation of histone H3K14 and non-canonical histone H3K23 in ethylene signalling.

Nature communications (2016-10-04)
Fan Zhang, Bin Qi, Likai Wang, Bo Zhao, Siddharth Rode, Nathaniel D Riggan, Joseph R Ecker, Hong Qiao
ABSTRACT

Ethylene gas is essential for many developmental processes and stress responses in plants. EIN2 plays a key role in ethylene signalling but its function remains enigmatic. Here, we show that ethylene specifically elevates acetylation of histone H3K14 and the non-canonical acetylation of H3K23 in etiolated seedlings. The up-regulation of these two histone marks positively correlates with ethylene-regulated transcription activation, and the elevation requires EIN2. Both EIN2 and EIN3 interact with a SANT domain protein named EIN2 nuclear associated protein 1 (ENAP1), overexpression of which results in elevation of histone acetylation and enhanced ethylene-inducible gene expression in an EIN2-dependent manner. On the basis of these findings we propose a model where, in the presence of ethylene, the EIN2 C terminus contributes to downstream signalling via the elevation of acetylation at H3K14 and H3K23. ENAP1 may potentially mediate ethylene-induced histone acetylation via its interactions with EIN2 C terminus.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-acetyl-Histone H4 Antibody, 1 mg/mL, Upstate®
Sigma-Aldrich
Anti-acetyl-Histone H3 (Lys14) Antibody, serum, Upstate®
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Anti-acetyl-Histone H3 (Lys27) Antibody, serum, Upstate®
Sigma-Aldrich
Anti-acetyl-Histone H3 Antibody, from rabbit
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Anti-acetyl-Histone H3 (Lys23) Antibody, serum, Upstate®
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Anti-acetyl-Histone H3 (Lys18) Antibody, serum, Upstate®
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Anti-acetyl-Histone H3 (Lys9) Antibody, serum, Upstate®