scholarly journals Activating and inhibitory functions for the histone lysine methyltransferase G9a in T helper cell differentiation and function

2010 ◽  
Vol 207 (5) ◽  
pp. 915-922 ◽  
Author(s):  
Bernhard Lehnertz ◽  
Jeffrey P. Northrop ◽  
Frann Antignano ◽  
Kyle Burrows ◽  
Sima Hadidi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Differentiation ◽  
Stem Cell Differentiation ◽  
T Helper ◽  
Trichuris Muris ◽  
Th Cells ◽  
Histone Lysine ◽  
Histone Lysine Methyltransferase ◽  
Lysine Methyltransferase ◽  
And Function

Accumulating evidence suggests that the regulation of gene expression by histone lysine methylation is crucial for several biological processes. The histone lysine methyltransferase G9a is responsible for the majority of dimethylation of histone H3 at lysine 9 (H3K9me2) and is required for the efficient repression of developmentally regulated genes during embryonic stem cell differentiation. However, whether G9a plays a similar role in adult cells is still unclear. We identify a critical role for G9a in CD4+ T helper (Th) cell differentiation and function. G9a-deficient Th cells are specifically impaired in their induction of Th2 lineage-specific cytokines IL-4, IL-5, and IL-13 and fail to protect against infection with the intestinal helminth Trichuris muris. Furthermore, G9a-deficient Th cells are characterised by the increased expression of IL-17A, which is associated with a loss of H3K9me2 at the Il17a locus. Collectively, our results establish unpredicted and complex roles for G9a in regulating gene expression during lineage commitment in adult CD4+ T cells.

Activating and inhibitory functions for the histone lysine methyltransferase G9a in T helper cell differentiation and function

2010 ◽  
Vol 189 (3) ◽  
pp. i9-i9
Author(s):  
Bernhard Lehnertz ◽  
Jeffrey P. Northrop ◽  
Frann Antignano ◽  
Kyle Burrows ◽  
Sima Hadidi ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
T Helper Cell ◽  
Helper Cell ◽  
T Helper ◽  
Histone Lysine ◽  
Histone Lysine Methyltransferase ◽  
Lysine Methyltransferase ◽  
And Function

scholarly journals The histone lysine methyltransferase KMT2D sustains a gene expression program that represses B cell lymphoma development

2015 ◽  
Vol 21 (10) ◽  
pp. 1199-1208 ◽  
Author(s):  
Ana Ortega-Molina ◽  
Isaac W Boss ◽  
Andres Canela ◽  
Heng Pan ◽  
Yanwen Jiang ◽  
...  
Keyword(s):  
Gene Expression ◽  
B Cell ◽  
Cell Lymphoma ◽  
B Cell Lymphoma ◽  
Gene Expression Program ◽  
Histone Lysine ◽  
Histone Lysine Methyltransferase ◽  
Lysine Methyltransferase ◽  
Expression Program

Essential Cytoplasmic Role of the Histone Lysine Methyltransferase Setdb1 in Post-Transcriptional Regulation in Embryonic Stem Cells

2021 ◽  
Author(s):  
Roberta Rapone ◽  
Laurence Del Maestro ◽  
Costas Bouyioukos ◽  
Sonia Albini ◽  
Paola Cruz-Tapias ◽  
...  
Keyword(s):  
Gene Expression ◽  
Stem Cells ◽  
Transcriptional Regulation ◽  
Mrna Stability ◽  
Regulation Of Gene Expression ◽  
Embryonic Stem ◽  
Histone Lysine ◽  
Histone Lysine Methyltransferase ◽  
Lysine Methyltransferase ◽  
Post Transcriptional Regulation

Abstract Embryonic stem cells (ESCs) fate is regulated both at transcriptional and post-transcriptional levels. Indeed, several studies showed that, in addition to gene transcription, mRNA stability and protein synthesis are finely tuned and strongly control the ESCs pluripotency and fate changes. An increasing number of RNA-binding proteins (RBPs) involved in post-transcriptional and translational regulation of gene expression has been identified as regulators of ESC identity. The major lysine methyltransferase Setdb1 is essential for the self-renewal and viability of ESCs. Setdb1 was primarily known to methylate the lysine 9 of histone 3 (H3K9) in the nucleus, where it regulates chromatin functions. However, Setdb1 is also massively localized in the cytoplasm, including in mouse ESCs, where its role remains unknown. Here we show that the cytoplasmic Setdb1 (cSetdb1) is essential for the survival of mESCs. Functional assays further demonstrate that cSetdb1 regulates gene expression post-transcriptionally, affecting the abundance of mRNAs and the rate of newly synthetized proteins. A yeast-two-hybrid assay shows that cSetdb1 interacts with several regulators of mRNA stability and protein translation machinery, such as the ESCs-specific E3 ubiquitin ligase and mRNA silencer Trim71/Lin41. Finally, proteomic analyses reveal that cSetdb1 is required for the integrity of Trim71 complexes involved in mRNA metabolism and translation. Altogether, our data uncover the essential cytoplasmic function of a firstly supposed nuclear “histone” lysine methyltransferase, Setdb1, and provide new insights into the cytoplasmic/post-transcriptional regulation of gene expression mediated by a key epigenetic regulator.

scholarly journals Histone Lysine Methyltransferase SDG8 Is Involved in Brassinosteroid-Regulated Gene Expression in Arabidopsis thaliana

2014 ◽  
Vol 7 (8) ◽  
pp. 1303-1315 ◽  
Author(s):  
Xiaolei Wang ◽  
Jiani Chen ◽  
Zhouli Xie ◽  
Sanzhen Liu ◽  
Trevor Nolan ◽  
...  
Keyword(s):  
Gene Expression ◽  
Arabidopsis Thaliana ◽  
Histone Lysine ◽  
Histone Lysine Methyltransferase ◽  
Lysine Methyltransferase ◽  
Regulated Gene Expression

Concentration-dependent gene expression responses to flusilazole in embryonic stem cell differentiation cultures

2011 ◽  
Vol 251 (2) ◽  
pp. 110-118 ◽  
Author(s):  
Dorien A.M. van Dartel ◽  
Jeroen L.A. Pennings ◽  
Liset J.J. de la Fonteyne ◽  
Karen J.J. Brauers ◽  
Sandra Claessen ◽  
...  
Keyword(s):  
Gene Expression ◽  
Stem Cell ◽  
Cell Differentiation ◽  
Embryonic Stem Cell ◽  
Embryonic Stem ◽  
Stem Cell Differentiation ◽  
Embryonic Stem Cell Differentiation

On the Histone Lysine Methyltransferase Activity of Fungal Metabolite Chaetocin

2013 ◽  
Vol 56 (21) ◽  
pp. 8616-8625 ◽  
Author(s):  
Fanny L. Cherblanc ◽  
Kathryn L. Chapman ◽  
Jim Reid ◽  
Aaron J. Borg ◽  
Sandeep Sundriyal ◽  
...  
Keyword(s):  
Fungal Metabolite ◽  
Methyltransferase Activity ◽  
Histone Lysine ◽  
Histone Lysine Methyltransferase ◽  
Lysine Methyltransferase
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