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Related Concept Videos

The Nucleosome01:19

The Nucleosome

Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
The Nucleosome02:33

The Nucleosome

DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...

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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

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Nuclear titin interacts with histones.

Lan King1, Chun-Ru Jhou

  • 1Department of Biochemistry and Molecular Biology, Collage of Medicine, Chang Gung University, Taoyuan, Taiwan. lanking@mail.cgu.edu.tw

Chang Gung Medical Journal
|May 5, 2010
PubMed
Summary

Nuclear titin, a giant muscle protein, was purified and found to interact with histones H2A, H3, and H4. This suggests titin may function as a chromosome scaffold in the nucleus.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Titin is a large muscle protein crucial for muscle elasticity.
  • Its role and presence within the cell nucleus were previously unconfirmed.

Purpose of the Study:

  • To investigate the presence and function of titin in the cell nucleus.
  • To identify proteins interacting with nuclear titin.

Main Methods:

  • Nuclear titin extraction and purification using buffer solutions and chromatography.
  • Mass spectrometry (MS) and MS/MS analyses to identify associated proteins.

Main Results:

  • Purified nuclear titin was obtained, confirming its presence in the nucleus.
  • Three low molecular weight proteins, identified as histones H2A, H3, and H4, strongly associated with titin.

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

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In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
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In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

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  • These histones were inseparable from titin via chromatography.

    • Conclusions:

    • The study confirms the existence of titin within the cell nucleus.
    • Nuclear titin demonstrates a strong interaction with histones H2A, H3, and H4.
    • This interaction suggests a potential role for titin as a chromosome scaffold.