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Related Concept Videos

The Nucleosome02:33

The Nucleosome

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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...
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The Nucleosome01:19

The Nucleosome

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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.
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Nucleosome Remodeling02:54

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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.
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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.
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Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
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Structure and function of the Orc1 BAH-nucleosome complex.

Pablo De Ioannes1, Victor A Leon2, Zheng Kuang3,4

  • 1Skirball Institute of Biomolecular Medicine, Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, 10016, USA.

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Summary

The Origin Recognition Complex (ORC) binds nucleosomes regardless of histone modifications, enabling its roles in both open and closed chromatin. This interaction is crucial for maintaining genome stability and rDNA border integrity during meiosis.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • The Origin Recognition Complex (ORC) is vital for eukaryotic DNA replication, heterochromatin formation, telomere maintenance, and genome stability.
  • Histone modifications, particularly acetylation of lysine 16 on histone H4 (H4K16), are key determinants of chromatin structure, distinguishing between open (euchromatin) and closed (heterochromatin) states.

Purpose of the Study:

  • To elucidate the structural basis of how the yeast Orc1 BAH domain interacts with nucleosomes.
  • To investigate whether Orc1 discriminates between modified and unmodified histone H4 tails, specifically H4K16 acetylation.
  • To explore the functional implications of Orc1's nucleosome interaction in chromatin regulation and genome stability.

Main Methods:

  • X-ray crystallography to determine the structure of the yeast Orc1 BAH domain bound to a nucleosome core particle.
  • Biochemical assays to assess Orc1's binding preference to nucleosomes with different histone H4 tail modifications.

Main Results:

  • The study presents the structure of the yeast Orc1 BAH domain in complex with a nucleosome core particle.
  • Orc1 does not discriminate between acetylated and non-acetylated H4K16, unlike the related protein Sir3.
  • Direct nucleosome interaction by Orc1 is essential for maintaining rDNA border integrity during meiosis, independent of its replication and silencing functions.

Conclusions:

  • Orc1's ability to bind nucleosomes irrespective of H4K16 modification state allows it to function in both hetero- and euchromatin.
  • This interaction is critical for maintaining genome stability, particularly at rDNA borders during meiosis.
  • The findings reveal a unique mechanism for Orc1's chromatin association and highlight its multifaceted roles beyond replication and silencing.