Identification and characterization of the interaction proteins of HISTONE DEACETYLASE 15
Date Issued
2015
Date
2015
Author(s)
Yeh, Pei-Ming
Abstract
Histone deacetylases (HDACs or HDAs) are responsible for the deacetylation of lysine residues on the N-terminal tail of core histones and play an important role in transcriptional regulation, cell cycle progression and developmental events. HISTONE DEACETYLASES 15 (HDA15), one of the RPD3/HDA1 superfamily members, is known to regulate chlorophyll biosynthesis and photosynthesis by interacting with PHYTOCHROME INTERACTING FACTOR3 (PIF3). We found that many proteins can interact with HDA15 by LC-MS/MS analysis. The interaction of HDA15 with these identified proteins was further confirmed by bimolecular fluorescence complementation assays. In particular, we found that HDA15 can interact with the MOS4 associated complex involved in plant immune responses. Similar to mos4-1, hda15 mutants were hypersensitive to Pseudomonas syringae pv. tomato DC3000 after three days inoculation, supporting that HDA15 may interact with the MOS4 associated complex to regulate plant immunity. BES1-INTERACTING MYC-LIKE PROTEINS 1 (BIM1), BIM2 and BIM3 belong to the bHLH protein family. BIMs interact with BR-INSENSITIVE-EMS-SUPPRESSOR1 (BES1) to synergistically bind to the E-boxes that are present in the promoter regions of a multitude of genes such as Brassinosteroid (BR) responding genes. It was reported that the simultaneous elimination of all three BIM proteins results in reduced BR-mediated responses. In this study, we found that BIM2 can interact with HDA15 and HDA6, and bim1/bim2/bim3 and axe1-5 accumulate less anthocyanin under high salt conditions and are hypersensitive to salt stress in the seed germination stage.
Subjects
Arabidopsis
histone deacetylases 15
MOS4 associated complex
plant immunity
Type
thesis
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