scholarly journals Site-specific Loss of Acetylation upon Phosphorylation of Histone H3

2002 ◽  
Vol 277 (33) ◽  
pp. 29496-29502 ◽  
Author(s):  
Diane G. Edmondson ◽  
Judith K. Davie ◽  
Jenny Zhou ◽  
Banafsheh Mirnikjoo ◽  
Kelly Tatchell ◽  
...  
Keyword(s):  
Histone H3 ◽  
Site Specific ◽  
Specific Loss

scholarly journals Crosstalk between site-specific modifications on p53 and histone H3

Oncogene ◽  
2007 ◽  
Vol 27 (11) ◽  
pp. 1639-1644 ◽  
Author(s):  
L J Warnock ◽  
R Adamson ◽  
C J Lynch ◽  
J Milner
Keyword(s):  
Histone H3 ◽  
Site Specific

scholarly journals Site-specific Acetylation of Histone H3 Decreases Polymerase β Activity on Nucleosome Core Particlesin Vitro

2016 ◽  
Vol 291 (21) ◽  
pp. 11434-11445 ◽  
Author(s):  
Yesenia Rodriguez ◽  
John M. Hinz ◽  
Marian F. Laughery ◽  
John J. Wyrick ◽  
Michael J. Smerdon
Keyword(s):  
Histone H3 ◽  
Site Specific ◽  
Nucleosome Core

scholarly journals The TAZ2 domain of CBP/p300 directs acetylation towards H3K27 within chromatin

2020 ◽  
Author(s):  
Thomas W. Sheahan ◽  
Viktoria Major ◽  
Kimberly M. Webb ◽  
Elana Bryan ◽  
Philipp Voigt
Keyword(s):  
Gene Expression ◽  
Stem Cells ◽  
Enzymatic Activity ◽  
Crucial Role ◽  
Regulation Of Gene Expression ◽  
Histone H3 ◽  
Embryonic Stem ◽  
Site Specific ◽  
Lysine Residues

AbstractThe closely related acetyltransferases CBP and p300 are key regulators of gene expression in metazoans. CBP/p300 acetylate several specific lysine residues within nucleosomes, including histone H3 lysine 27 (H3K27), a hallmark of active enhancers and promoters. However, it has remained largely unclear how specificity of CBP/p300 towards H3K27 is achieved. Here we show that the TAZ2 domain of CBP is required for efficient acetylation of H3K27, while curbing activity towards other lysine residues within nucleosomes. We find that TAZ2 is a sequence-independent DNA binding module, promoting interaction between CBP and nucleosomes, thereby enhancing enzymatic activity and regulating substrate specificity of CBP. TAZ2 is further required to stabilize CBP binding to chromatin in mouse embryonic stem cells, facilitating specificity towards H3K27 and modulating gene expression. These findings reveal a crucial role of TAZ2 in regulating H3K27ac, while highlighting the importance of correct site-specific acetylation for proper regulation of gene expression.

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

Uteroplacental insufficiency induces site-specific changes in histone H3 covalent modifications and affects DNA-histone H3 positioning in day 0 IUGR rat liver

2004 ◽  
Vol 20 (1) ◽  
pp. 108-116 ◽  
Author(s):  
Qi Fu ◽  
Robert A. McKnight ◽  
Xing Yu ◽  
Laiyi Wang ◽  
Christopher W. Callaway ◽  
...  
Keyword(s):  
Histone H3 ◽  
Site Specific ◽  
Promoter Sequences ◽  
Histone Deacetylase 1 ◽  
Protein Levels ◽  
Ppar Γ ◽  
Covalent Modifications ◽  
A Site ◽  
H3 Acetylation ◽  
Carnitine Palmitoyl Transferase I

Uteroplacental insufficiency and subsequent intrauterine growth retardation (IUGR) increase the risk of adult onset insulin resistance and dyslipidemia in humans and rats. IUGR rats are further characterized by postnatal alterations in hepatic PPAR-γ coactivator (PGC-1) and carnitine-palmitoyl-transferase I (CPTI) expression, as well as overall hyperacetylation of histone H3. However, it is unknown whether the histone H3 hyperacetylation is site specific or relates to the changes in gene expression previously described in IUGR rats. We therefore hypothesized that uteroplacental insufficiency causes site-specific modifications in hepatic H3 acetylation and affects the association of acetylated histone H3 with PGC-1 and CPTI promoter sequences. Uteroplacental insufficiency was used to produce asymmetrical IUGR rats. IUGR significantly increased acetylation of H3 lysine-9 (H3/K9), lysine-14 (H3/K14), and lysine-18 (H3/K18) at day 0 of life, and these changes occurred in association with decreased nuclear protein levels of histone deacetylase 1 (HDAC1) and HDAC activity. Chromatin immunoprecipitation using acetyl-H3/K9 antibody and day 0 chromatin revealed that uteroplacental insufficiency affected the association between acetylated H3/K9 and the promoters of PGC-1 and CPTI, respectively, in IUGR liver. At day 21 of life, the neonatal pattern of H3 hyperacetylation persisted only in the IUGR males. We conclude that uteroplacental insufficiency increases H3 acetylation in a site-specific manner in IUGR liver and that these changes persist in male IUGR animals. The altered association of the PGC-1 and CPTI promoters with acetylated H3/K9 correlates with previous reports of IUGR altering the expression of these genes. We speculate that in utero alterations of chromatin structure contribute to fetal programming.

Relationship between site-specific loss of thigh muscle and gait performance in women: The HIREGASAKI study

2012 ◽  
Vol 55 (2) ◽  
pp. e21-e25 ◽  
Author(s):  
Takashi Abe ◽  
Madoka Ogawa ◽  
Jeremy P. Loenneke ◽  
Robert S. Thiebaud ◽  
Mark Loftin ◽  
...  
Keyword(s):  
Thigh Muscle ◽  
Site Specific ◽  
Gait Performance ◽  
Specific Loss

scholarly journals Histone H3 Clipping is a novel signature of Human Neutrophil Extracellular Traps

2021 ◽  
Author(s):  
Dorothea Ogmore Tilley ◽  
Ulrike Abuabed ◽  
Ursula Zimny Arndt ◽  
Monika Schmid ◽  
Stefan Florian ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Neurological Disease ◽  
Histone H3 ◽  
Neutrophil Extracellular Traps ◽  
Mixed Cell ◽  
Site Specific ◽  
Tissue Sections ◽  
Extracellular Traps ◽  
Subsequent Degradation ◽  
Regulatory Functions

Neutrophils are critical to host defence, executing diverse strategies to perform their antimicrobial and regulatory functions. One tactic is the production of neutrophil extracellular traps (NETs). In response to certain stimuli neutrophils decondense their lobulated nucleus and release chromatin into the extracellular space through a process called NETosis. However, NETosis, and the subsequent degradation of NETs, can become dysregulated. NETs are proposed to play a role in infectious as well as many non-infection related diseases including cancer, thrombosis, autoimmunity and neurological disease. Consequently, there is a need to develop specific tools for the study of these structures in disease contexts. In this study, we identified a NET-specific histone H3 cleavage event and harnessed this to develop a cleavage site-specific antibody for the detection of human NETs. By microscopy, this antibody distinguishes NETs from chromatin in purified and mixed cell samples. It also detects NETs in tissue sections. We propose this antibody as a new tool to detect and quantify NETs.

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