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  4. Arabidopsis histone H3 lysine 9 methyltransferases KYP/SUVH5/6 are involved in leaf development by interacting with AS1-AS2 to repress KNAT1 and KNAT2
 
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Arabidopsis histone H3 lysine 9 methyltransferases KYP/SUVH5/6 are involved in leaf development by interacting with AS1-AS2 to repress KNAT1 and KNAT2

Journal
Communications biology
Journal Volume
6
Journal Issue
1
Pages
219
Date Issued
2023-02-24
Author(s)
Hung, Fu-Yu
Feng, Yun-Ru
Hsin, Kuan-Ting
Shih, Yuan-Hsin
Chang, Chung-Han
Zhong, Wenjian
Lai, You-Cheng
Xu, Yingchao
Yang, Songguang
Sugimoto, Keiko
YI-SHENG CHENG  
KEQIANG WU  
DOI
10.1038/s42003-023-04607-6
URI
https://scholars.lib.ntu.edu.tw/handle/123456789/629208
URL
https://api.elsevier.com/content/abstract/scopus_id/85148965834
Abstract
The Arabidopsis H3K9 methyltransferases KRYPTONITE/SUPPRESSOR OF VARIEGATION 3-9 HOMOLOG 4 (KYP/SUVH4), SUVH5 and SUVH6 are redundantly involved in silencing of transposable elements (TEs). Our recent study indicated that KYP/SUVH5/6 can directly interact with the histone deacetylase HDA6 to synergistically regulate TE expression. However, the function of KYP/SUVH5/6 in plant development is still unclear. The transcriptional factors ASYMMETRIC LEAVES1 (AS1) and AS2 form a transcription complex, which is involved in leaf development by repressing the homeobox genes KNOTTED-LIKE FROM ARABIDOPSIS THALIANA 1 (KNAT1) and KNAT2. In this study, we found that KYP and SUVH5/6 directly interact with AS1-AS2 to repress KNAT1 and KNAT2 by altering histone H3 acetylation and H3K9 dimethylation levels. In addition, KYP can directly target the promoters of KNAT1 and KNAT2, and the binding of KYP depends on AS1. Furthermore, the genome-wide occupancy profile of KYP indicated that KYP is enriched in the promoter regions of coding genes, and the binding of KYP is positively correlated with that of AS1 and HDA6. Together, these results indicate that Arabidopsis H3K9 methyltransferases KYP/SUVH5/6 are involved in leaf development by interacting with AS1-AS2 to alter histone H3 acetylation and H3K9 dimethylation from KNAT1 and KNAT2 loci.
SDGs

[SDGs]SDG2

[SDGs]SDG13

Publisher
NLM (Medline)
Type
journal article

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