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Related Concept Videos

Histone Modification02:32

Histone Modification

15.9K
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
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Histone Modification02:32

Histone Modification

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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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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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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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.
Writers
The writer...
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Inheritance of Chromatin Structures03:17

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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Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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Sirtuin 6 is a histone delactylase.

Garrison A Nickel1, Nicholas J Pederson1, Faheem1

  • 1Department of Medicinal Chemistry, University of Utah, Salt Lake City, Utah, USA.

The Journal of Biological Chemistry
|October 8, 2025
PubMed
Summary

Sirtuin 6 (Sirt6) removes histone lactylation (Kla), a modification linked to gene expression. This discovery reveals a new mechanism for regulating gene expression by controlling histone lactylation levels.

Keywords:
epigeneticshistone deacetylasehistone lactylationhistone modificationslactic acidsirtuin

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Simultaneous Measurement of HDAC1 and HDAC6 Activity in HeLa Cells Using UHPLC-MS
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Area of Science:

  • Biochemistry
  • Epigenetics
  • Molecular Biology

Background:

  • Histone lactylation (Kla) is a post-translational modification (PTM) derived from metabolic lactate.
  • Kla is involved in inflammation resolution, macrophage polarization, differentiation, wound repair, and oncogenesis.
  • Mechanisms linking Kla to gene expression regulation are not well understood.

Purpose of the Study:

  • To identify novel histone delactylase enzymes.
  • To characterize the histone delactylase activity of Sirtuin 6 (Sirt6).
  • To investigate the role of Sirt6 in regulating gene expression via histone lactylation.

Main Methods:

  • In vitro assays to assess Sirt6's histone delactylase activity.
  • Mammalian cell culture models to study Sirt6's function in vivo.
  • Mass spectrometry to identify lactylated histone sites targeted by Sirt6.

Main Results:

  • Sirt6 exhibits histone delactylase activity.
  • Sirt6 removes histone lactylation at H3K9 and H3K18.
  • Sirt6 and Class I HDACs display distinct, non-overlapping delactylase activities.

Conclusions:

  • Sirt6 is a novel histone delactylase, targeting H3K9 and H3K18.
  • Sirt6 represents a distinct pathway for regulating gene expression through histone lactylation.
  • Sirt6 and Class I HDACs offer complementary mechanisms for controlling histone lactylation levels.