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POWERDRESS and HDA9 interact and promote histone H3 deacetylation at specific genomic sites in Arabidopsis

Title
POWERDRESS and HDA9 interact and promote histone H3 deacetylation at specific genomic sites in Arabidopsis
Authors
Kim, YJ[Kim, Yun Ju]Wang, RZ[Wang, Ruozhong]Gao, L[Gao, Lei]Li, DM[Li, Dongming]Xu, C[Xu, Chi]Mang, HG[Mang, Hyunggon]Jeon, JE[Jeon, Jien]Chen, XS[Chen, Xiangsong]Zhong, XH[Zhong, Xuehua]Kwak, JM[Kwak, June M.]Mo, BX[Mo, Beixin]Xiao, LT[Xiao, Langtao]Chen, XM[Chen, Xuemei]
DGIST Authors
Kwak, JM[Kwak, June M.]
Issue Date
2016-12-20
Citation
Proceedings of the National Academy of Sciences of the United States of America, 113(51), 14858-14863
Type
Article
Article Type
Article
Keywords
AGL19HDA9Histone DeacetylationPOWERDRESSSant Domain
ISSN
0027-8424
Abstract
Histone acetylation is a major epigenetic control mechanism that is tightly linked to the promotion of gene expression. Histone acetylation levels are balanced through the opposing activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Arabidopsis HDAC genes (AtHDACs) compose a large gene family, and distinct phenotypes among AtHDAC mutants reflect the functional specificity of individual AtHDACs. However, the mechanisms underlying this functional diversity are largely unknown. Here, we show that POWERDRESS (PWR), a SANT (SWI3/DAD2/N-CoR/TFIII-B) domain protein, interacts with HDA9 and promotes histone H3 deacetylation, possibly by facilitating HDA9 function at target regions. The developmental phenotypes of pwr and hda9 mutants were highly similar. Three lysine residues (K9, K14, and K27) of H3 retained hyperacetylation status in both pwr and hda9 mutants. Genome-wide H3K9 and H3K14 acetylation profiling revealed elevated acetylation at largely overlapping sets of target genes in the two mutants. Highly similar gene-expression profiles in the two mutants correlated with the histone H3 acetylation status in the pwr and hda9 mutants. In addition, PWR and HDA9 modulated flowering time by repressing AGAMOUS-LIKE 19 expression through histone H3 deacetylation in the same genetic pathway. Finally, PWR was shown to physically interact with HDA9, and its SANT2 domain, which is homologous to that of subunits in animal HDAC complexes, showed specific binding affinity to acetylated histone H3. We therefore propose that PWR acts as a subunit in a complex with HDA9 to result in lysine deacetylation of histone H3 at specific genomic targets. © 2016, National Academy of Sciences. All rights reserved.
URI
http://hdl.handle.net/20.500.11750/2103
DOI
10.1073/pnas.1618618114
Publisher
National Academy of Sciences
Related Researcher
  • Author Kwak, June Myoung KWAK_LAB(Lab of Cell Signailng)
  • Research Interests Calcium Signaling; ABA;ROS Signaling; drought-tolerant plants; Development of Abscission; Culluar Features; Signaling network; Environmental Regulation
Files:
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Collection:
New BiologyETC1. Journal Articles


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