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Related Concept Videos

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.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Histone Modification02:32

Histone Modification

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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
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Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening

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Structure and function of histone acetyltransferase MOF.

Qiao Yi Chen1, Max Costa1, Hong Sun1

  • 1Department of Environmental Medicine, NYU School of Medicine, Tuxedo, NY, USA.

AIMS Biophysics
|May 16, 2017
PubMed
Summary

The male-specific lethal complex member MOF (male-specific lethal complex component MSL, also known as MYST1) is a histone acetyltransferase. This review discusses hMOF

Keywords:
H4K16MOFMSLNSLhistone acetylation

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Biochemistry

Background:

  • The MOF protein, initially identified in Drosophila melanogaster, is a key component of the dosage compensation complex.
  • As a member of the MYST family of histone acetyltransferases, MOF specifically targets histone H4 lysine 16 for acetylation.
  • Mammalian orthologs of MOF have conserved substrate specificity and enzymatic activities, highlighting its evolutionary importance.

Purpose of the Study:

  • To review the structure and activity of mammalian hMOF.
  • To discuss the role of hMOF in H4K16 acetylation, DNA damage response, and stem cell pluripotency.
  • To explore the implications of hMOF dysregulation in human carcinogenesis.

Main Methods:

  • Literature review of existing studies on MOF and hMOF.
  • Analysis of conserved features and functions across species.
  • Synthesis of data on hMOF's involvement in various cellular processes and diseases.

Main Results:

  • hMOF is crucial for regulating gene expression, DNA repair, and maintaining stem cell pluripotency.
  • Specific acetylation of H4K16 by hMOF is a key mechanism in its diverse functions.
  • Dysregulation of hMOF is linked to the development and progression of various human cancers.

Conclusions:

  • hMOF plays a vital role in fundamental biological processes, including epigenetic regulation and DNA damage response.
  • Understanding hMOF's functions offers insights into potential therapeutic strategies for cancer.
  • Further research into hMOF's mechanisms can illuminate its broader roles in health and disease.