scholarly journals The function of histone lysine methylation related SET domain group proteins in plants

2020 ◽  
Vol 29 (5) ◽  
pp. 1120-1137
Author(s):  
Huiyan Zhou ◽  
Yanhong Liu ◽  
Yuwei Liang ◽  
Dong Zhou ◽  
Shuifeng Li ◽  
...  
Keyword(s):  
Lysine Methylation ◽  
Set Domain ◽  
Histone Lysine Methylation ◽  
Histone Lysine

scholarly journals Genome-wide analysis of SET-domain group histone methyltransferases in apple reveals their role in development and stress responses

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Wenjie Li ◽  
Jinjiao Yan ◽  
Shicong Wang ◽  
Qianying Wang ◽  
Caixia Wang ◽  
...  
Keyword(s):  
Stress Responses ◽  
Sequence Similarity ◽  
Expression Profiles ◽  
Expression Patterns ◽  
Lysine Methylation ◽  
Set Domain ◽  
Histone Methyltransferases ◽  
Histone Lysine Methylation ◽  
Histone Lysine ◽  
Genome Wide

Abstract Background Histone lysine methylation plays an important role in plant development and stress responses by activating or repressing gene expression. Histone lysine methylation is catalyzed by a class of SET-domain group proteins (SDGs). Although an increasing number of studies have shown that SDGs play important regulatory roles in development and stress responses, the functions of SDGs in apple remain unclear. Results A total of 67 SDG members were identified in the Malus×domestica genome. Syntenic analysis revealed that most of the MdSDG duplicated gene pairs were associated with a recent genome-wide duplication event of the apple genome. These 67 MdSDG members were grouped into six classes based on sequence similarity and the findings of previous studies. The domain organization of each MdSDG class was characterized by specific patterns, which was consistent with the classification results. The tissue-specific expression patterns of MdSDGs among the 72 apple tissues in the different apple developmental stages were characterized to provide insight into their potential functions in development. The expression profiles of MdSDGs were also investigated in fruit development, the breaking of bud dormancy, and responses to abiotic and biotic stress; the results indicated that MdSDGs might play a regulatory role in development and stress responses. The subcellular localization and putative interaction network of MdSDG proteins were also analyzed. Conclusions This work presents a fundamental comprehensive analysis of SDG histone methyltransferases in apple and provides a basis for future studies of MdSDGs involved in apple development and stress responses.

scholarly journals Dynamic Patterns of Histone Lysine Methylation in the Developing Retina

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

The Indexing Potential of Histone Lysine Methylation

2008 ◽  
pp. 22-47 ◽  
Author(s):  
Gunnar Schotta ◽  
Monika Lachner ◽  
Antoine H. F. M. Peters ◽  
Thomas Jenuwein
Keyword(s):  
Lysine Methylation ◽  
Histone Lysine Methylation ◽  
Histone Lysine

scholarly journals Protein lysine 43 methylation by EZH1 promotes AML1-ETO transcriptional repression in leukemia

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Liping Dou ◽  
Fei Yan ◽  
Jiuxia Pang ◽  
Dehua Zheng ◽  
Dandan Li ◽  
...  
Keyword(s):  
Dna Sequences ◽  
Transcriptional Repression ◽  
Lysine Methylation ◽  
Post Translational Modification ◽  
Histone Lysine Methylation ◽  
Histone Lysine ◽  
Histone Lysine Methyltransferase ◽  
Lysine Methyltransferase

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.

Histone lysine methylation exhibits a distinct distribution during spermatogenesis in pigs

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

Impacts of Histone Lysine Methylation on Chromatin

2016 ◽  
pp. 25-53
Author(s):  
S. Lanouette ◽  
J. Haddad ◽  
P. Zhang ◽  
J.-F. Couture
Keyword(s):  
Lysine Methylation ◽  
Histone Lysine Methylation ◽  
Histone Lysine
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