scholarly journals Structural Basis of LSD1-CoREST Selectivity in Histone H3 Recognition

2007 ◽  
Vol 282 (28) ◽  
pp. 20070-20074 ◽  
Author(s):  
Federico Forneris ◽  
Claudia Binda ◽  
Antonio Adamo ◽  
Elena Battaglioli ◽  
Andrea Mattevi
Keyword(s):  
Histone H3 ◽  
Structural Basis

scholarly journals Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase

2019 ◽  
Vol 33 (11-12) ◽  
pp. 620-625 ◽  
Author(s):  
Seongmin Jang ◽  
Chanshin Kang ◽  
Han-Sol Yang ◽  
Taeyang Jung ◽  
Hans Hebert ◽  
...  
Keyword(s):  
Histone H3 ◽  
Structural Basis ◽  
Histone H2b

scholarly journals Structural basis of nucleosomal histone H4 lysine 20 methylation by SET8 methyltransferase

2021 ◽  
Vol 4 (4) ◽  
pp. e202000919
Author(s):  
Cheng-Han Ho ◽  
Yoshimasa Takizawa ◽  
Wataru Kobayashi ◽  
Yasuhiro Arimura ◽  
Hiroshi Kimura ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Essential Role ◽  
Histone H3 ◽  
Underlying Mechanism ◽  
Structural Basis ◽  
Histone H4 ◽  
Nucleosomal Histone

SET8 is solely responsible for histone H4 lysine-20 (H4K20) monomethylation, which preferentially occurs in nucleosomal H4. However, the underlying mechanism by which SET8 specifically promotes the H4K20 monomethylation in the nucleosome has not been elucidated. Here, we report the cryo-EM structures of the human SET8–nucleosome complexes with histone H3 and the centromeric H3 variant, CENP-A. Surprisingly, we found that the overall cryo-EM structures of the SET8–nucleosome complexes are substantially different from the previous crystal structure models. In the complexes with H3 and CENP-A nucleosomes, SET8 specifically binds the nucleosomal acidic patch via an arginine anchor, composed of the Arg188 and Arg192 residues. Mutational analyses revealed that the interaction between the SET8 arginine anchor and the nucleosomal acidic patch plays an essential role in the H4K20 monomethylation activity. These results provide the groundwork for understanding the mechanism by which SET8 specifically accomplishes the H4K20 monomethylation in the nucleosome.

scholarly journals Structural Basis for the Specific Recognition of Methylated Histone H3 Lysine 4 by the WD-40 Protein WDR5

2006 ◽  
Vol 22 (1) ◽  
pp. 137-144 ◽  
Author(s):  
Zhifu Han ◽  
Lan Guo ◽  
Huayi Wang ◽  
Yue Shen ◽  
Xing Wang Deng ◽  
...  
Keyword(s):  
Histone H3 ◽  
Structural Basis ◽  
Specific Recognition

The structural basis of human Spt16 N-terminal domain interaction with histone (H3-H4)2 tetramer

2019 ◽  
Vol 508 (3) ◽  
pp. 864-870
Author(s):  
Hua Jiang ◽  
Sidan Xu ◽  
Yiping Chen ◽  
Huiyan Li ◽  
Lu Tian ◽  
...  
Keyword(s):  
Histone H3 ◽  
Structural Basis ◽  
Domain Interaction ◽  
Terminal Domain

scholarly journals Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger

Cell Research ◽  
2011 ◽  
Vol 21 (9) ◽  
pp. 1379-1382 ◽  
Author(s):  
Chengkun Wang ◽  
Jie Shen ◽  
Zhongzheng Yang ◽  
Ping Chen ◽  
Bin Zhao ◽  
...  
Keyword(s):  
Histone H3 ◽  
Structural Basis ◽  
Site Specific ◽  
Phd Finger ◽  
Specific Reading

scholarly journals Structural Basis of a Histone H3 Lysine 4 Demethylase Required for Stem Elongation in Rice

PLoS Genetics ◽  
2013 ◽  
Vol 9 (1) ◽  
pp. e1003239 ◽  
Author(s):  
Qingfeng Chen ◽  
Xiangsong Chen ◽  
Quan Wang ◽  
Faben Zhang ◽  
Zhiyong Lou ◽  
...  
Keyword(s):  
Stem Elongation ◽  
Histone H3 ◽  
Structural Basis

scholarly journals Structural basis of the regulation of normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2

2020 ◽  
Author(s):  
Ko Sato ◽  
Amarjeet Kumar ◽  
Keisuke Hamada ◽  
Chikako Okada ◽  
Asako Oguni ◽  
...  
Keyword(s):  
Histone H3 ◽  
Point Mutations ◽  
Polycomb Group ◽  
Structural Basis ◽  
Nucleosomal Dna ◽  
Oncogenic Mutations ◽  
Repressive Effect ◽  
Binding Cleft ◽  
Dynamics Simulations ◽  
Nucleosome Binding

SummaryDimethylated histone H3 Lys36 (H3K36me2) regulates gene expression by antagonizing the repressive effect of polycomb-group proteins. Aberrant upregulation of H3K36me2, either by overexpression or point mutations of NSD2/MMSET, an H3K36 dimethyltransferase, is found in various cancers, including multiple myeloma. To understand the mechanism underlying its regulation, here we report the cryo-electron microscopy structure of the catalytic fragment of NSD2 bound to the nucleosome at 2.8 Å resolution. The nucleosomal DNA is partially unwrapped at superhelix location +5.5, facilitating the access of NSD2 to H3K36. NSD2 interacts with DNA and H2A along with H3. The autoinhibitory loop of NSD2 changes its conformation upon nucleosome binding to accommodate H3 in its substrate-binding cleft. Kinetic analysis revealed two oncogenic mutations, E1099K and T1150A, to aberrantly activate NSD2 by increasing its catalytic turnover but not the nucleosome affinity. Molecular dynamics simulations suggested that in both mutants, the autoinhibitory loop adopts an open state that can accommodate H3 more often than the wild type. We propose that E1099K and T1150A destabilize the interactions that keep the autoinhibitory loop closed, thereby enhancing the catalytic turnover. Our analyses would guide the development of specific inhibitors of NSD2 for the treatment of various cancers.

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