Barley Lunasin Suppressesras-Induced Colony Formation and Inhibits Core Histone Acetylation in Mammalian Cells

2002 ◽  
Vol 50 (21) ◽  
pp. 5903-5908 ◽  
Author(s):  
Hyung J. Jeong ◽  
Yi Lam ◽  
Ben O. de Lumen
Keyword(s):  
Histone Acetylation ◽  
Colony Formation ◽  
Mammalian Cells ◽  
Core Histone

The cancer preventive peptide lunasin from wheat inhibits core histone acetylation

2007 ◽  
Vol 255 (1) ◽  
pp. 42-48 ◽  
Author(s):  
Hyung Jin Jeong ◽  
Jin Boo Jeong ◽  
Dae Seop Kim ◽  
Jae Ho Park ◽  
Jung Bok Lee ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Core Histone

Relationship between Core Histone Acetylation and Histone H10 Gene Activity

1994 ◽  
Vol 224 (3) ◽  
pp. 885-892 ◽  
Author(s):  
Valerie Girardot ◽  
Thierry Rabilloud ◽  
Minoru Yoshida ◽  
Teruhiko Beppu ◽  
Jean-Jacques Lawrence ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Gene Activity ◽  
Core Histone

scholarly journals Developmental activation of the lysozyme gene in chicken macrophage cells is linked to core histone acetylation at its enhancer elements

2006 ◽  
Vol 34 (14) ◽  
pp. 4025-4035 ◽  
Author(s):  
Fiona A. Myers ◽  
Pascal Lefevre ◽  
Evangelia Mantouvalou ◽  
Kimberley Bruce ◽  
Claire Lacroix ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Core Histone ◽  
Lysozyme Gene ◽  
Macrophage Cells ◽  
Chicken Macrophage

Isoflavones stimulate estrogen receptor-mediated core histone acetylation

2004 ◽  
Vol 317 (1) ◽  
pp. 259-264 ◽  
Author(s):  
Tao Hong ◽  
Takeya Nakagawa ◽  
WeiJun Pan ◽  
Mi Young Kim ◽  
W Lee Kraus ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Histone Acetylation ◽  
Core Histone

scholarly journals Dynamic Analysis of Proviral Induction and De Novo Methylation: Implications for a Histone Deacetylase-Independent, Methylation Density-Dependent Mechanism of Transcriptional Repression

2000 ◽  
Vol 20 (3) ◽  
pp. 842-850 ◽  
Author(s):  
Matthew C. Lorincz ◽  
Dirk Schübeler ◽  
Scott C. Goeke ◽  
Mark Walters ◽  
Mark Groudine ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Histone Acetylation ◽  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Mammalian Cells ◽  
Fluorescent Protein ◽  
De Novo ◽  
Trichostatin A ◽  
Histone Deacetylation ◽  
Over Time

ABSTRACT Methylation of cytosines in the CpG dinucleotide is generally associated with transcriptional repression in mammalian cells, and recent findings implicate histone deacetylation in methylation-mediated repression. Analyses of histone acetylation in in vitro-methylated transfected plasmids support this model; however, little is known about the relationships among de novo DNA methylation, transcriptional repression, and histone acetylation state. To examine these relationships in vivo, we have developed a novel approach that permits the isolation and expansion of cells harboring expressing or silent retroviruses. MEL cells were infected with a Moloney murine leukemia virus encoding the green fluorescent protein (GFP), and single-copy, silent proviral clones were treated weekly with the histone deacetylase inhibitor trichostatin A or the DNA methylation inhibitor 5-azacytidine. Expression was monitored concurrently by flow cytometry, allowing for repeated phenotypic analysis over time, and proviral methylation was determined by Southern blotting and bisulfite methylation mapping. Shortly after infection, proviral expression was inducible and the reporter gene and proviral enhancer showed a low density of methylation. Over time, the efficacy of drug induction diminished, coincident with the accumulation of methyl-CpGs across the provirus. Bisulfite analysis of cells in which 5-azacytidine treatment induced GFP expression revealed measurable but incomplete demethylation of the provirus. Repression could be overcome in late-passage clones only by pretreatment with 5-azacytidine followed by trichostatin A, suggesting that partial demethylation reestablishes the trichostatin-inducible state. These experiments reveal the presence of a silencing mechanism which acts on densely methylated DNA and appears to function independently of histone deacetylase activity.

scholarly journals Disruption of Higher-Order Folding by Core Histone Acetylation Dramatically Enhances Transcription of Nucleosomal Arrays by RNA Polymerase III

1998 ◽  
Vol 18 (8) ◽  
pp. 4629-4638 ◽  
Author(s):  
Christin Tse ◽  
Takashi Sera ◽  
Alan P. Wolffe ◽  
Jeffrey C. Hansen
Keyword(s):  
Rna Polymerase ◽  
Histone Acetylation ◽  
Molecular Mechanisms ◽  
Chromatin Condensation ◽  
Rna Polymerase Iii ◽  
Higher Order ◽  
Core Histone ◽  
Rrna Gene ◽  
Histone Octamer ◽  
Polymerase Iii

ABSTRACT We have examined the effects of core histone acetylation on the transcriptional activity and higher-order folding of defined 12-mer nucleosomal arrays. Purified HeLa core histone octamers containing an average of 2, 6, or 12 acetates per octamer (8, 23, or 46% maximal site occupancy, respectively) were assembled onto a DNA template consisting of 12 tandem repeats of a 208-bp Lytechinus 5S rRNA gene fragment. Reconstituted nucleosomal arrays were transcribed in a Xenopus oocyte nuclear extract and analyzed by analytical hydrodynamic and electrophoretic approaches to determine the extent of array compaction. Results indicated that in buffer containing 5 mM free Mg2+ and 50 mM KCl, high levels of acetylation (12 acetates/octamer) completely inhibited higher-order folding and concurrently led to a 15-fold enhancement of transcription by RNA polymerase III. The molecular mechanisms underlying the acetylation effects on chromatin condensation were investigated by analyzing the ability of differentially acetylated nucleosomal arrays to fold and oligomerize. In MgCl2-containing buffer the folding of 12-mer nucleosomal arrays containing an average of two or six acetates per histone octamer was indistinguishable, while a level of 12 acetates per octamer completely disrupted the ability of nucleosomal arrays to form higher-order folded structures at all ionic conditions tested. In contrast, there was a linear relationship between the extent of histone octamer acetylation and the extent of disruption of Mg2+-dependent oligomerization. These results have yielded new insight into the molecular basis of acetylation effects on both transcription and higher-order compaction of nucleosomal arrays.

Chromosomal Mapping of Core Histone Acetylation by Immunoselection

Methods ◽  
1997 ◽  
Vol 12 (1) ◽  
pp. 48-56 ◽  
Author(s):  
Colyn Crane-Robinson ◽  
Tim R. Hebbes ◽  
Alison L. Clayton ◽  
Alan W. Thorne
Keyword(s):  
Histone Acetylation ◽  
Chromosomal Mapping ◽  
Core Histone
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