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Related Concept Videos

Histone Modification02:32

Histone Modification

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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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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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Co-activators and Co-repressors02:04

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Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
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NF-κB-dependent Signaling Pathway02:26

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The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
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Inheritance of Chromatin Structures

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Structural insights into the HNF4 biology.

Brice Beinsteiner1,2,3,4, Isabelle M L Billas1,2,3,4, Dino Moras1,2,3,4

  • 1Laboratory IGBMC (Institute of Genetics and of Molecular and Cellular Biology), Centre for Integrative Biology (CBI), Illkirch, France.

Frontiers in Endocrinology
|July 5, 2023
PubMed
Summary

Hepatocyte Nuclear Factor 4 (HNF4) is a key transcription factor regulating liver genes. This review examines HNF4 structures, disease links, and how mutations and modifications impact its function.

Keywords:
DNA AllosteryHNF4MODY1hepatocyte nuclear factor 4nuclear receptorsprotein-DNA complexesstructural biologytranscription

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Hepatocyte Nuclear Factor 4 (HNF4) is a crucial transcription factor (TF) in the nuclear receptor (NR) family.
  • It plays a vital role in liver-specific gene expression, particularly for lipid and glucose metabolism, and is essential for development.
  • HNF4 dysregulation is implicated in diseases like type I diabetes (MODY1) and hemophilia.

Purpose of the Study:

  • To review the structures of the DNA binding domain (DBD) and ligand binding domain (LBD) of HNF4.
  • To compare HNF4 structures with other nuclear receptors.
  • To discuss HNF4α biology from a structural viewpoint, focusing on mutations and post-translational modifications.

Main Methods:

  • Structural analysis of isolated HNF4 DNA binding domain (DBD) and ligand binding domain (LBD).
  • Comparison of HNF4 structures with other nuclear receptors.
  • Review of existing literature on HNF4α mutations and post-translational modifications.

Main Results:

  • Detailed comparison of HNF4 DBD and LBD structures with other NRs.
  • Insights into how pathological mutations affect HNF4 structure and function.
  • Understanding the impact of post-translational modifications on HNF4α receptor activity.

Conclusions:

  • Structural insights into HNF4 are critical for understanding its regulatory roles.
  • Pathological mutations and post-translational modifications significantly influence HNF4 structure-function relationships.
  • This review provides a structural perspective on HNF4 biology and its disease relevance.