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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...
DNA Packaging00:58

DNA Packaging

Overview
DNA Packaging00:58

DNA Packaging

Overview
Genomic DNA in Eukaryotes00:58

Genomic DNA in Eukaryotes

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.
Chromatin Packaging02:21

Chromatin Packaging

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? 
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order structures.

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Related Experiment Video

Updated: May 8, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

TFAM organizes DNA into compact higher order structures.

Sashi R Weerawarana1, Wei Tian1,2, Karolin Luger1,2

  • 1Department of biochemistry, University of Colorado, Boulder, CO, USA.

Biorxiv : the Preprint Server for Biology
|May 7, 2026
PubMed
Summary
This summary is machine-generated.

Transcription Factor A, Mitochondrial (TFAM) organizes mitochondrial DNA (mtDNA) into nucleoids. This study reveals TFAM oligomerization on longer DNA forms compact, dynamic structures, clarifying its genome organization role.

Keywords:
Major classification: Biological sciencesMinor classification: BiochemistryTFAMbiophysics and computational biologycryo-EMmass photometrymitochondria

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Area of Science:

  • Mitochondrial biology
  • Molecular genetics
  • Structural biology

Background:

  • Transcription Factor A, Mitochondrial (TFAM) is crucial for mitochondrial DNA (mtDNA) homeostasis.
  • TFAM's role in mtDNA transcription is studied, but its genome organization function is less understood.
  • Existing models of TFAM-DNA interaction use short DNA fragments, not reflecting in vivo nucleoid formation.

Purpose of the Study:

  • To investigate TFAM oligomerization on longer DNA fragments.
  • To characterize the structural basis of TFAM-mediated mtDNA compaction.
  • To elucidate the mechanism of mitochondrial nucleoid formation.

Main Methods:

  • Biochemical analysis of TFAM-DNA interactions.
  • Structural analysis of TFAM oligomers on DNA.
  • Cryo-electron microscopy (cryo-EM) for low-resolution structural insights.

Main Results:

  • TFAM oligomerizes on longer DNA segments, forming higher-order complexes.
  • These complexes are homogenous and exhibit continuous conformational dynamics.
  • Cryo-EM suggests a regular organization within mitochondrial nucleoids.

Conclusions:

  • TFAM utilizes oligomerization to compact mtDNA into higher-order structures.
  • This study provides insights into the mechanism of mitochondrial nucleoid organization.
  • Findings lay the groundwork for understanding TFAM's role in mtDNA stability and disease.