نتایج جستجو برای: histone acetylation

تعداد نتایج: 49569  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1998
W A Krajewski P B Becker

Increased acetylation at specific N-terminal lysines of core histones is a hallmark of active chromatin in vivo, yet the structural consequences of acetylation leading to increased gene activity are only poorly defined. We employed a new approach to characterize the effects of histone acetylation: A Drosophila embryo-derived cell-free system for chromatin reconstitution under physiological cond...

2011
Nilanjana Chatterjee Divya Sinha Mekonnen Lemma-Dechassa Song Tan Michael A. Shogren-Knaak Blaine Bartholomew

There is a close relationship between histone acetylation and ATP-dependent chromatin remodeling that is not fully understood. We show that acetylation of histone H3 tails affects SWI/SNF (mating type switching/ sucrose non fermenting) and RSC (remodels structure of chromatin) remodeling in several distinct ways. Acetylation of the histone H3 N-terminal tail facilitated recruitment and nucleoso...

Journal: :Molecular & Cellular Proteomics 2002

2014
Qiao Li Michelle Foote Jihong Chen

The tight interaction between genomic DNA and histones, which normally represses gene transcription, can be relaxed by histone acetylation. This loosening of the DNA-histone complex is important for selective gene activation during stem cell differentiation. Histone acetylation may be increased through the application of histone deacetylase inhibitors at the early stages of differentiation to m...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2008
Shanshan Li Michael A Shogren-Knaak

Acetylation of histone proteins by the yeast Spt-Ada-Gcn5-acetyltansferase (SAGA) complex has served as a paradigm for understanding how posttranslational modifications of chromatin regulate eukaryotic gene expression. Nonetheless, it has been unclear to what extent the structural complexity of the chromatin substrate modulates SAGA activity. By using chromatin model systems, we have found that...

Journal: :Molecular pharmacology 2005
Jane L Rose Hong Huang Scott F Wray Dale G Hoyt

Engagement of integrin cell adhesion receptors in mouse lung endothelial cells induces global sensitivity of DNA to nuclease digestion, reflecting alterations in chromatin structure. These structural changes may contribute to the antigenotoxic effects of integrin engagement in lung endothelium. Because histone acetylation and poly(ADP-ribosyl)ation modulate chromatin structure, we investigated ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2015
Alison E Ringel Anne M Cieniewicz Sean D Taverna Cynthia Wolberger

The Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator complex hyperacetylates histone tails in vivo in a manner that depends upon histone 3 lysine 4 trimethylation (H3K4me3), a histone mark enriched at promoters of actively transcribed genes. SAGA contains a separable subcomplex known as the histone acetyltransferase (HAT) module that contains the HAT, Gcn5, bound to Sgf29, Ada2, and Ada3. Sgf2...

Journal: :The Biochemical journal 1991
M J Hendzel J R Davie

The relationship between histone acetylation and methylation in chicken immature erythrocytes was investigated. Previous studies have shown that transcriptionally active/competent gene-enriched chromatin fragments are enriched in newly methylated histones H3 and H4. Moreover, newly methylated histone H4 is hyperacetylated. Here, we show that dynamically acetylated histone H4 is selectively enga...

2012
Katja Merschbaecher Jakob Haettig Uli Mueller

Learning induced changes in protein acetylation, mediated by histone acetyl transferases (HATs), and the antagonistic histone deacetylases (HDACs) play a critical role in memory formation. The status of histone acetylation affects the interaction between the transcription-complex and DNA and thus regulates transcription-dependent processes required for long-term memory (LTM). While the majority...

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