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Related Concept Videos

Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Spreading of Chromatin Modifications02:25

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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...
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Histone Modification02:32

Histone Modification

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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.
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The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Abnormal Proliferation02:23

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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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Epigenetic Regulation01:37

Epigenetic Regulation

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Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...
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Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
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Histone H3.3 and cancer: A potential reader connection.

Fei Lan1, Yang Shi2

  • 1Key Laboratory of Epigenetics of Shanghai Ministry of Education, School of Basic Medicine and Institutes of Biomedical Sciences, Shanghai Medical College of Fudan University, Shanghai 200032, China; Key Laboratory of Birth Defect, Children's Hospital of Fudan University, Shanghai 201102, China; yshi@hms.harvard.edu fei_lan@fudan.edu.cn.

Proceedings of the National Academy of Sciences of the United States of America
|December 3, 2014
PubMed
Summary
This summary is machine-generated.

Histone H3.3 mutations are linked to pediatric cancers. The BS69 protein specifically binds to a modified form of H3.3, and cancer mutations may disrupt this interaction, impacting tumor suppression.

Keywords:
BS69H3.3H3.3K36me3cancerhistone

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Area of Science:

  • Molecular Biology
  • Cancer Biology
  • Epigenetics

Background:

  • Nucleosomes, composed of DNA and histone proteins, are the fundamental units of chromatin.
  • Somatic missense mutations in the histone H3 variant, H3.3, are implicated in various pediatric and young-adult cancers.
  • The precise mechanisms by which H3.3 mutations contribute to tumorigenesis remain largely unknown.

Purpose of the Study:

  • To investigate the role of BS69/ZMYND11 in relation to H3.3 and its potential involvement in tumor suppression.
  • To explore how H3.3 cancer mutations affect interactions with cellular factors like BS69.

Main Methods:

  • Literature review of recent studies identifying BS69/ZMYND11 as an H3.3K36me3 reader.
  • Analysis of predicted effects of H3.3 cancer mutations on the H3.3K36me3/BS69 interaction.

Main Results:

  • BS69/ZMYND11 was identified as a specific binding partner for the modified histone H3.3 (H3.3K36me3).
  • Certain H3.3 cancer mutations are predicted to disrupt the interaction between H3.3K36me3 and BS69.
  • This disruption suggests a potential role for the H3.3K36me3/BS69 interaction in tumor suppression.

Conclusions:

  • The interaction between H3.3K36me3 and BS69 is a significant finding with potential implications for tumor suppression.
  • H3.3 cancer mutations may contribute to tumorigenesis by disrupting this interaction or altering other cellular factor interactions.