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Related Concept Videos

Epigenetic Regulation01:46

Epigenetic Regulation

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Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
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Epigenetic Regulation01:37

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Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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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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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
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Related Experiment Video

Updated: Nov 20, 2025

Electrophoretic Mobility Shift Assay EMSA for the Study of RNA-Protein Interactions: The IRE/IRP Example
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Epigenomic regulation by labile iron.

Vladimir Camarena1, Tyler C Huff2, Gaofeng Wang3

  • 1John P. Hussman Institute for Human Genomics, Dr. John T. Macdonald Foundation Department of Human Genetics, University of Miami Miller School of Medicine, Miami, FL, 33136, USA.

Free Radical Biology & Medicine
|January 25, 2021
PubMed
Summary

Intracellular labile iron, a small pool of iron in cells, plays a key role in regulating gene expression and cellular metabolism. New probes help us understand its function in epigenetics and signaling pathways.

Keywords:
DNA methylationG-protein coupled receptorHistone methylationIntracellular labile Fe(II)IronJmjC domain-containing demethylasesRapGEF2Reactive oxygen speciesTET methylcytosine DioxygenasescAMP

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Area of Science:

  • Cellular biology
  • Biochemistry
  • Epigenetics

Background:

  • Iron is essential for cellular functions but can cause oxidative damage.
  • Intracellular labile iron (ILI) is a small, redox-active fraction of cellular iron.
  • Quantifying ILI has been challenging, limiting our understanding of its roles.

Purpose of the Study:

  • To examine the role of ILI in epigenetic regulation.
  • To investigate how ILI modulates histone and DNA demethylation.
  • To explore ILI's function as a signaling mediator.

Main Methods:

  • Development and application of novel intracellular labile iron probes.
  • Analysis of ILI's impact on histone and DNA demethylation processes.
  • Investigation of ILI's role in cAMP-mediated signaling pathways.

Main Results:

  • Recent advances in ILI probes enable better quantification and understanding.
  • ILI has been discovered to regulate the epigenome.
  • ILI influences histone and DNA demethylation pathways.

Conclusions:

  • Intracellular labile iron is crucial for epigenetic regulation.
  • ILI acts as a signaling hub, connecting metabolic status to cellular responses.
  • Further research using advanced probes will uncover more functions of ILI.