期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 51, 页码 14858-14863出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1618618114
关键词
SANT domain; POWERDRESS; HDA9; histone deacetylation; AGL19
资金
- NIH [GM061146]
- Gordon and Betty Moore Foundation [GBMF3046]
- Guangdong Innovation Research Team Fund [2014ZT05S078]
- National Natural Science Foundation of China [31570372, 31671777]
- National Science Foundation CAREER Award [MCB-1552455]
- Alexander von Humboldt Foundation (Alfred Toepfer Faculty Fellow Award)
- National Institute of Food and Agriculture [1002874]
- US Department of Agriculture
- [IBS-R013-G2]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1552455] Funding Source: National Science Foundation
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.
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