scholarly journals Histone tales: lysine methylation, a protagonist in Arabidopsis development

Author(s):  
Kai Cheng ◽  
Yingchao Xu ◽  
Chao Yang ◽  
Luc Ouellette ◽  
Longjian Niu ◽  
...  

Recent advances in the regulation of histone lysine methylation in plants and the role of this modification in the developmental programming of Arabidopsis are discussed.

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Qiaoyan Guo ◽  
Xiaoxia Li ◽  
Hongbo Han ◽  
Chaoyuan Li ◽  
Shujun Liu ◽  
...  

Transforming growth factor beta1- (TGF-β1-) induced p21-dependent mesangial cell (MC) hypertrophy plays a key role in the pathogenesis of chronic renal diseases including diabetic nephropathy (DN). Increasing evidence demonstrated the role of posttranscriptional modifications (PTMs) in the event; however, the precise regulatory mechanism of histone lysine methylation remains largely unknown. Here, we examined the roles of both histone H3 lysine 4 and lysine 9 methylations (H3K4me/H3K9me) in TGF-β1 induced p21 gene expression in rat mesangial cells (RMCs). Our results indicated that TGF-β1 upregulated the expression of p21 gene in RMCs, which was positively correlated with the increased chromatin marks associated with active genes (H3K4me1/H3K4me2/H3K4me3) and negatively correlated with the decreased levels of repressive marks (H3K9me2/H3K9me3) at p21 gene promoter. TGF-β1 also elevated the recruitment of the H3K4 methyltransferase (HMT) SET7/9 to the p21 gene promoter. SET7/9 gene silencing with small interfering RNAs (siRNAs) significantly abolished the TGF-β1 induced p21 gene expression. Taken together, these results reveal the key role of histone H3Kme in TGF-β1 mediated p21 gene expression in RMC, partly through HMT SET7/9 occupancy, suggesting H3Kme and SET7/9 may be potential renoprotective agents in managing chronic renal diseases.


2021 ◽  
Vol 12 ◽  
Author(s):  
Elena Di Nisio ◽  
Giuseppe Lupo ◽  
Valerio Licursi ◽  
Rodolfo Negri

Eukaryotic genomes are wrapped around nucleosomes and organized into different levels of chromatin structure. Chromatin organization has a crucial role in regulating all cellular processes involving DNA-protein interactions, such as DNA transcription, replication, recombination and repair. Histone post-translational modifications (HPTMs) have a prominent role in chromatin regulation, acting as a sophisticated molecular code, which is interpreted by HPTM-specific effectors. Here, we review the role of histone lysine methylation changes in regulating the response to radiation-induced genotoxic damage in mammalian cells. We also discuss the role of histone methyltransferases (HMTs) and histone demethylases (HDMs) and the effects of the modulation of their expression and/or the pharmacological inhibition of their activity on the radio-sensitivity of different cell lines. Finally, we provide a bioinformatic analysis of published datasets showing how the mRNA levels of known HMTs and HDMs are modulated in different cell lines by exposure to different irradiation conditions.


2010 ◽  
Vol 51 (12) ◽  
pp. 6784 ◽  
Author(s):  
Rajesh C. Rao ◽  
Kissaou T. Tchedre ◽  
Muhammad Taimur A. Malik ◽  
Natasha Coleman ◽  
Yuan Fang ◽  
...  

Author(s):  
Gunnar Schotta ◽  
Monika Lachner ◽  
Antoine H. F. M. Peters ◽  
Thomas Jenuwein

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Liping Dou ◽  
Fei Yan ◽  
Jiuxia Pang ◽  
Dehua Zheng ◽  
Dandan Li ◽  
...  

Abstract The oncogenic fusion protein AML1-ETO retains the ability of AML1 to interact with the enhancer core DNA sequences, but blocks AML1-dependent transcription. Previous studies have shown that post-translational modification of AML1-ETO may play a role in its regulation. Here we report that AML1-ETO-positive patients, with high histone lysine methyltransferase Enhancer of zeste homolog 1 (EZH1) expression, show a worse overall survival than those with lower EZH1 expression. EZH1 knockdown impairs survival and proliferation of AML1-ETO-expressing cells in vitro and in vivo. We find that EZH1 WD domain binds to the AML1-ETO NHR1 domain and methylates AML1-ETO at lysine 43 (Lys43). This requires the EZH1 SET domain, which augments AML1-ETO-dependent repression of tumor suppressor genes. Loss of Lys43 methylation by point mutation or domain deletion impairs AML1-ETO-repressive activity. These findings highlight the role of EZH1 in non-histone lysine methylation, indicating that cooperation between AML1-ETO and EZH1 and AML1-ETO site-specific lysine methylation promote AML1-ETO transcriptional repression in leukemia.


2015 ◽  
Vol 84 (9) ◽  
pp. 1455-1462 ◽  
Author(s):  
Junhui An ◽  
Jinzhou Qin ◽  
Yi Wan ◽  
Yaqing Zhang ◽  
Yuan Hu ◽  
...  

Author(s):  
S. Lanouette ◽  
J. Haddad ◽  
P. Zhang ◽  
J.-F. Couture

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