Arabidopsis SUMO E3 Ligase SIZ1 Interacts with HDA6 and Negatively Regulates HDA6 Function during Flowering

The changes in histone acetylation mediated by histone deacetylases (HDAC) play a crucial role in plant development and response to environmental changes. Mammalian HDACs are regulated by post-translational modifications (PTM), such as phosphorylation, acetylation, ubiquitination and small ubiquitin...

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Published inCells (Basel, Switzerland) Vol. 10; no. 11; p. 3001
Main Authors Gao, Sujuan, Zeng, Xueqin, Wang, Jianhao, Xu, Yingchao, Yu, Chunwei, Huang, Yishui, Wang, Feng, Wu, Keqiang, Yang, Songguang
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 03.11.2021
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Summary:The changes in histone acetylation mediated by histone deacetylases (HDAC) play a crucial role in plant development and response to environmental changes. Mammalian HDACs are regulated by post-translational modifications (PTM), such as phosphorylation, acetylation, ubiquitination and small ubiquitin-like modifier (SUMO) modification (SUMOylation), which affect enzymatic activity and transcriptional repression. Whether PTMs of plant HDACs alter their functions are largely unknown. In this study, we demonstrated that the SUMO E3 ligase SAP AND MIZ1 DOMAIN-CONTAINING LIGASE1 (SIZ1) interacts with HISTONE DEACETYLASE 6 (HDA6) both in vitro and in vivo. Biochemical analyses indicated that HDA6 is not modified by SUMO1. Overexpression of in background results in a decreased level of histone H3 acetylation, indicating that the activity of HDA6 is increased in plants. Chromatin immunoprecipitation (ChIP) assays showed that SIZ1 represses HDA6 binding to its target genes ( ) and ( ), resulting in the upregulation of and by increasing the level of histone H3 acetylation. Together, these findings indicate that the SUMO E3 ligase SIZ1 interacts with HDA6 and negatively regulates HDA6 function.
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These authors contributed equally to this work.
ISSN:2073-4409
2073-4409
DOI:10.3390/cells10113001