scholarly journals Structural Insights into Histone H3 Lysine 56 Acetylation by Rtt109

Structure ◽  
2008 ◽  
Vol 16 (10) ◽  
pp. 1503-1510 ◽  
Author(s):  
Chengqi Lin ◽  
Y. Adam Yuan
Keyword(s):  
Histone H3 ◽  
Structural Insights

Structural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase

2006 ◽  
Vol 359 (1) ◽  
pp. 86-96 ◽  
Author(s):  
Chengmin Qian ◽  
Xueqi Wang ◽  
Karishma Manzur ◽  
Sachchidanand ◽  
Amjad Farooq ◽  
...  
Keyword(s):  
Histone H3 ◽  
Structural Insights

scholarly journals Structural Insights for MPP8 Chromodomain Interaction with Histone H3 Lysine 9: Potential Effect of Phosphorylation on Methyl-Lysine Binding

2011 ◽  
Vol 408 (5) ◽  
pp. 807-814 ◽  
Author(s):  
Yanqi Chang ◽  
John R. Horton ◽  
Mark T. Bedford ◽  
Xing Zhang ◽  
Xiaodong Cheng
Keyword(s):  
Histone H3 ◽  
Potential Effect ◽  
Structural Insights

scholarly journals Structural insights into selective histone H3 recognition by the human Polybromo bromodomain 2

Cell Research ◽  
2010 ◽  
Vol 20 (5) ◽  
pp. 529-538 ◽  
Author(s):  
Zachary Charlop-Powers ◽  
Lei Zeng ◽  
Qiang Zhang ◽  
Ming-Ming Zhou
Keyword(s):  
Histone H3 ◽  
Structural Insights

scholarly journals Structural insights into the recognition of histone H3Q5 serotonylation by WDR5

2021 ◽  
Vol 7 (25) ◽  
pp. eabf4291
Author(s):  
Jie Zhao ◽  
Wanbiao Chen ◽  
Yi Pan ◽  
Yinfeng Zhang ◽  
Huiying Sun ◽  
...  
Keyword(s):  
Posttranslational Modification ◽  
Gene Activation ◽  
Histone H3 ◽  
Neuroblastoma Cells ◽  
Neuronal Cell ◽  
Promoter Regions ◽  
Unknown Mechanism ◽  
Neuronal Cell Differentiation ◽  
Induce Cell Proliferation ◽  
Structural Insights

Serotonylation of histone H3Q5 (H3Q5ser) is a recently identified posttranslational modification of histones that acts as a permissive marker for gene activation in synergy with H3K4me3 during neuronal cell differentiation. However, any proteins that specifically recognize H3Q5ser remain unknown. Here, we found that WDR5 interacts with the N-terminal tail of histone H3 and functions as a “reader” for H3Q5ser. Crystal structures of WDR5 in complex with H3Q5ser and H3K4me3Q5ser peptides revealed that the serotonyl group is accommodated in a shallow surface pocket of WDR5. Experiments in neuroblastoma cells demonstrate that H3K4me3 modification is hampered upon disruption of WDR5-H3Q5ser interaction. WDR5 colocalizes with H3Q5ser in the promoter regions of cancer-promoting genes in neuroblastoma cells, where it promotes gene transcription to induce cell proliferation. Thus, beyond revealing a previously unknown mechanism through which WDR5 reads H3Q5ser to activate transcription, our study suggests that this WDR5-H3Q5ser–mediated epigenetic regulation apparently promotes tumorigenesis.

scholarly journals Structural insights into the recognition of histone H3Q5 serotonylation by WDR5

2020 ◽  
Author(s):  
Jie Zhao ◽  
Wanbiao Chen ◽  
Yinfeng Zhang ◽  
Fan Yang ◽  
Nan Shen ◽  
...  
Keyword(s):  
Posttranslational Modification ◽  
Gene Activation ◽  
Histone H3 ◽  
Neuroblastoma Cells ◽  
Neuronal Cell ◽  
Promoter Regions ◽  
Unknown Mechanism ◽  
Neuronal Cell Differentiation ◽  
Induce Cell Proliferation ◽  
Structural Insights

AbstractSerotonylation of histone H3Q5 (H3Q5ser) is a recently identified posttranslational modification of histones that apparently acts as a permissive marker for gene activation in synergy with H3K4me3 during neuronal cell differentiation. However, any proteins which specifically recognize H3Q5ser remain unknown. Here, we discovered that WDR5 interacts with the N-terminal tail of histone H3 and functions as a ‘reader’ for H3Q5ser. Crystal structures of WDR5 in complex with H3Q5ser and H3K4me3Q5ser peptides revealed that the serotonyl group is accommodated in a shallow surface pocket of WDR5. Experiments in neuroblastoma cells demonstrate that WDR5 colocalizes with H3Q5ser in the promoter regions of cancer-promoting genes, where it promotes gene transcription to induce cell proliferation. Thus, beyond revealing a previously unknown mechanism through which WDR5 reads H3Q5ser to activate transcription, our study suggests that this WDR5-H3Q5ser mediated epigenetic regulation apparently promotes tumorigenesis.

Structural insights into the interactions of Polycomb Repressive Complex 2 with chromatin

2021 ◽  
Author(s):  
Akhil Gargey Iragavarapu ◽  
Liqi Yao ◽  
Vignesh Kasinath
Keyword(s):  
Target Genes ◽  
Histone H3 ◽  
Cell Type ◽  
Methyltransferase Activity ◽  
Post Translational Modifications ◽  
Polycomb Repressive Complex 2 ◽  
Polycomb Proteins ◽  
Polycomb Repressive Complexes ◽  
Structural Insights ◽  
Stimulation Of

Polycomb repressive complexes are a family of chromatin modifier enzymes which are critical for regulating gene expression and maintaining cell-type identity. The reversible chemical modifications of histone H3 and H2A by the Polycomb proteins are central to its ability to function as a gene silencer. PRC2 is both a reader and writer of the tri-methylation of histone H3 lysine 27 (H3K27me3) which serves as a marker for transcription repression, and heterochromatin boundaries. Over the last few years, several studies have provided key insights into the mechanisms regulating the recruitment and activation of PRC2 at Polycomb target genes. In this review, we highlight the recent structural studies which have elucidated the roles played by Polycomb cofactor proteins in mediating crosstalk between histone post-translational modifications and the recruitment of PRC2 and the stimulation of PRC2 methyltransferase activity.

Expression of histone H3, p53, cyclin D1, and cyclin B1 in oral mucosal lesions

2009 ◽  
Vol 13 (4) ◽  
pp. 119-126
Author(s):  
Yoshimitsu Bamba ◽  
Tetsunari Nishikawa ◽  
Akio Tanaka
Keyword(s):  
Cyclin D1 ◽  
Histone H3 ◽  
Cyclin B1 ◽  
Oral Mucosal Lesions ◽  
Mucosal Lesions
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