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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.
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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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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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The biological clock is involved in many aspects of regulating complex physiology in all animals. It was in 1935 when German zoologists, Hans Kalmus and Erwin Bünning, discovered the existence of circadian rhythm in Drosophila melanogaster. However, the internal molecular mechanisms behind the circadian clock remained a mystery until 1984, when Jeffrey C. Hall, Michael Rosbash, and Michael W. Young discovered the expression of the Per gene oscillating over a 24-hour cycle. In subsequent...
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In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
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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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Bidirectional histone monoaminylation dynamics regulate neural rhythmicity.

Qingfei Zheng1,2, Benjamin H Weekley3, David A Vinson3

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Summary

Transglutaminase 2 (TG2) modifies histone H3 at Gln5 with various chemical groups, including histaminylation. This epigenetic mark regulates gene expression, circadian rhythms, and behavior in the brain.

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Area of Science:

  • Epigenetics
  • Neuroscience
  • Molecular Biology

Background:

  • Histone H3 monoaminylations at Gln5 (H3Q5) are crucial epigenetic marks for gene expression in the brain.
  • Transglutaminase 2 (TG2) catalyzes serotonylation (H3Q5ser) and dopaminylation (H3Q5dop) of H3Q5, impacting chromatin states.

Purpose of the Study:

  • To investigate TG2's role in H3 monoaminylation beyond serotonylation and dopaminylation.
  • To explore the function of H3Q5 histaminylation (H3Q5his) in the brain.
  • To elucidate the regulatory mechanisms of circadian gene expression and behavior.

Main Methods:

  • Biochemical assays to determine TG2's enzymatic activities.
  • Chromatin immunoprecipitation to analyze H3Q5 modifications.
  • Studies on gene expression, circadian rhythms, and behavior in animal models.

Main Results:

  • TG2 also functions as an eraser and exchanger of H3 monoaminylations, including H3Q5his.
  • H3Q5his exhibits diurnal rhythmicity in the brain and influences circadian gene expression and behavior.
  • H3Q5his antagonizes H3K4 methyltransferase activity by inhibiting WDR5 binding, unlike H3Q5ser.

Conclusions:

  • TG2 integrates chemical signals to modulate epigenetic states, impacting neural rhythmicity.
  • H3Q5 monoaminylations represent a dynamic epigenetic layer regulated by TG2.
  • The interplay between different H3Q5 modifications fine-tunes gene expression and neural functions.