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Related Concept Videos

Chromatin Packaging02:21

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Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
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Each human somatic cell contains 6 billion base pairs of DNA. Each base pair is 0.34 nm long, meaning each diploid cell contains a staggering 2 meters of DNA. This long DNA strand is packed inside a nucleus measuring only 10-20 microns in diameter with the help of specialized DNA-binding proteins called histones. Together they form a compact DNA-protein complex called chromatin. The chromatin is further compacted into higher-order structures. The highest level of compaction is achieved during...
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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.
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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Chromatin is the massive complex of DNA and proteins packaged inside the nucleus. The complexity of chromatin folding and how it is packaged inside the nucleus greatly influences  access to genetic information. Generally, the nucleus' periphery is considered transcriptionally repressive, while the cell's interior is considered a transcriptionally active area. 
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Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Chemical chromatin ubiquitylation.

Muhammad Jbara1, Hao Sun1, Guy Kamnesky1

  • 1Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 3200008, Israel.

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Summary

Chemical protein synthesis enables the creation of modified histone proteins for studying epigenetics. These histone analogues help researchers understand the role of ubiquitylation in DNA accessibility and gene regulation.

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Area of Science:

  • Biochemistry
  • Epigenetics
  • Molecular Biology

Background:

  • Histone modifications are crucial for regulating chromatin structure and DNA accessibility.
  • Access to DNA is essential for numerous cellular processes.
  • Chemical protein synthesis offers a method for producing modified histones.

Purpose of the Study:

  • To review the application of chemical protein synthesis in generating ubiquitylated histones.
  • To highlight the utility of these histone analogues in epigenetic research.
  • To explore the role of histone ubiquitylation in DNA-related processes.

Main Methods:

  • Total chemical protein synthesis
  • Semisynthetic approaches
  • Generation of ubiquitylated histone analogues

Main Results:

  • Homogeneously modified histone analogues can be produced in sufficient quantities.
  • These analogues facilitate biochemical, functional, and structural studies.
  • The utility of synthesized ubiquitylated histones in decoding epigenetic roles is demonstrated.

Conclusions:

  • Chemical protein synthesis is a powerful tool for creating essential histone analogues.
  • Ubiquitylated histone analogues are valuable for understanding epigenetic mechanisms.
  • This approach advances research into the functional significance of histone modifications.