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Related Concept Videos

Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer is an enzyme that can...
Hypoxia01:23

Hypoxia

Hypoxia is a medical condition characterized by an inadequate oxygen supply to body tissues. It typically manifests as a bluish discoloration of the skin and mucosae, especially in fair-skinned individuals, when hemoglobin (Hb) saturation drops below 75%.
Types of Hypoxia
There are four primary types of hypoxia, each resulting from a different cause:
1. Anemic hypoxia: This type occurs due to insufficient oxygen delivery caused by a lack of red blood cells (RBCs) or RBCs with abnormal or...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
Heterochromatin02:38

Heterochromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...

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Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
11:06

Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae

Published on: December 29, 2017

c-Myc mediates a hypoxia-induced decrease in acetylated histone H4.

Qin Li1, Max Costa

  • 1New York University School of Medicine, Nelson Institute of Environmental Medicine, Tuxedo, NY 10987, USA.

Biochimie
|July 15, 2009
PubMed
Summary
This summary is machine-generated.

Hypoxia, or low oxygen, decreases histone H4 acetylation (AcH4) and c-Myc protein levels in lung cancer cells. This reduction in c-Myc may explain how hypoxia represses gene expression.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Global histone H4 acetylation (AcH4) is a key epigenetic mark associated with gene transcriptional activation.
  • The c-Myc transcription factor plays a crucial role in regulating gene expression by binding to DNA and inducing AcH4.

Purpose of the Study:

  • To investigate the effect of hypoxia on AcH4 and c-Myc levels in human lung carcinoma (A549) and bronchial epithelial (Beas-2B) cells.
  • To elucidate the relationship between hypoxia, c-Myc, and AcH4 in the context of gene regulation.

Main Methods:

  • Exposure of A549 and Beas-2B cells to hypoxic conditions (1% Oxygen) for 24 hours.
  • Quantification of global AcH4 and c-Myc protein levels using molecular biology techniques.

Main Results:

  • Hypoxia significantly decreased both global AcH4 and c-Myc protein levels in A549 and Beas-2B cells.
  • The decline in AcH4 under hypoxia was more pronounced in A549 cells compared to Beas-2B cells.
  • The observed alterations in global AcH4 were directly correlated with decreased c-Myc protein levels.

Conclusions:

  • Hypoxia down-regulates global histone H4 acetylation, potentially through a reduction in c-Myc protein levels.
  • Decreased c-Myc levels induced by hypoxia may represent a mechanism for hypoxia-induced gene repression, complementing known hypoxia-induced gene activation pathways mediated by Hypoxia Response Elements (HRE).