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Related Concept Videos

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Eukaryotes have large genomes compared to prokaryotes. To fit their genomes into a cell, eukaryotic DNA is packaged extraordinarily tightly inside the nucleus. To achieve this, DNA is tightly wound around proteins called histones, which are packaged into nucleosomes that are joined by linker DNA and coil into chromatin fibers. Additional fibrous proteins further compact the chromatin, which is recognizable as chromosomes during certain phases of cell division.
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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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Super-resolution imaging reveals nucleolar encapsulation by single-stranded DNA.

Koichiro Maki1,2,3,4, Jumpei Fukute1,3, Taiji Adachi1,2,3,4

  • 1Laboratory of Biomechanics, Institute for Life and Medical Sciences, Kyoto University, 53 Shogoin-Kawahara, Sakyo, Kyoto 606-8507, Japan.

Journal of Cell Science
|August 29, 2024
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Summary

Nuclear bodies like the nucleolus are structurally maintained by a single-stranded DNA (ssDNA) complex. This ssDNA complex, with histone H1, encapsulates the nucleolus, ensuring genomic processes are coordinated within the nucleus.

Keywords:
In situ imagingDNA–protein interactionNucleolusNucleusSingle-stranded DNASuper-resolution imaging

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Area of Science:

  • Cell Biology
  • Genomics
  • Molecular Biology

Background:

  • Nuclear bodies, such as the nucleolus, are crucial for genomic processes.
  • The nucleolus is essential for ribosome biogenesis, involving proteins like RNA polymerase I and nucleophosmin 1 (NPM1).
  • While liquid-liquid phase separation (LLPS) is implicated in nucleolar formation, its structural maintenance within the nucleus is unclear.

Purpose of the Study:

  • To investigate the structural maintenance of the nucleolus within the intranuclear architecture.
  • To identify the molecular components responsible for the structural integrity of nuclear bodies.

Main Methods:

  • Super-resolution lattice-structured illumination microscopy (lattice-SIM) to visualize ssDNA distribution.
  • In situ digestion of ssDNA to assess its role in nucleolar structure.
  • Identification of ssDNA-binding proteins associated with nucleolar encapsulation.

Main Results:

  • The nucleolus is encapsulated by a molecular complex based on single-stranded DNA (ssDNA).
  • High abundance of ssDNA was observed surrounding the nucleolus.
  • Digestion of ssDNA led to nucleolar disruption and release of NPM1, confirming ssDNA's structural role.
  • ssDNA was found to form a complex with histone H1 for nucleolar encapsulation.

Conclusions:

  • The nucleolus's structural integrity is maintained by an ssDNA-based molecular complex.
  • This ssDNA-histone H1 complex provides encapsulation for nuclear bodies.
  • This mechanism is vital for coordinating nuclear genomic processes like transcription and replication.