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Related Concept Videos

Nitric Oxide Signaling Pathway01:28

Nitric Oxide Signaling Pathway

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Nitric oxide (NO), an inorganic gas, acts as a potent second messenger in most animal and plant tissues. NO diffuses out of the cells that produce it and enters the neighboring cells to generate a downstream response. NO synthase (NOS) catalyzes NO production by the deamination of the amino acid arginine. There are three isoforms of NOS. Endothelial cells have endothelial NOS (eNOS), nerve and muscle cells have neuronal NOS (nNOS), and macrophages produce inducible NOS (iNOS) upon exposure...
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Histone Modification02:32

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
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Spreading of Chromatin Modifications02:25

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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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The Nucleosome Core Particle01:12

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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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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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Related Experiment Video

Updated: Apr 29, 2026

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
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Nitric oxide and histone acetylation-shaping craniofacial development.

Libera Berghella1, Pier Lorenzo Puri2

  • 1Epigenetics & Regenerative Medicine, IRCCS Fondazione Santa Lucia, 00142 Rome, Italy.

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|May 27, 2014
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Summary

Nitric oxide (NO) and histone acetylation are crucial for craniofacial development. Disruptions in this signaling network may cause craniofacial malformations in humans.

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Area of Science:

  • Biochemistry
  • Developmental Biology
  • Molecular Biology

Background:

  • Nitric oxide (NO) signaling is linked to histone deacetylases (HDACs) in regulating tissue homeostasis.
  • Deregulation of NO-HDAC signaling is implicated in various human diseases.

Purpose of the Study:

  • To investigate the role of coordinated nitric oxide (NO) signaling and histone acetylation in cranial neural crest development.
  • To explore the contribution of NO/acetylation network alterations to craniofacial malformation pathogenesis.

Main Methods:

  • The study builds upon previous work linking NO signaling to HDACs.
  • It examines the coordinated action of NO signaling and histone acetylation.

Main Results:

  • Coordinated NO signaling and histone acetylation are essential for proper cranial neural crest development.
  • These processes are critical for craniofacial morphogenesis.

Conclusions:

  • The NO/acetylation network plays a vital role in craniofacial development.
  • Alterations in this network can contribute to the development of craniofacial malformations.