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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.
Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
Heterochromatin02:38

Heterochromatin

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.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Histone Modification02:32

Histone Modification

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 deacetylase,...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...

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Expression Analysis of Mammalian Linker-histone Subtypes
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Expression Analysis of Mammalian Linker-histone Subtypes

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Linker H1 Histone Direct Top-Down Proteoform Analysis.

Md Shofiul Alam1, Cassandra N Fuller1, Kevin Jeanne Dit Fouque1

  • 1Department of Chemistry and Biochemistry, Florida International University, Miami, Florida 33199, United States.

Journal of Proteome Research
|September 23, 2025
PubMed
Summary
This summary is machine-generated.

We developed a novel mass spectrometry method to directly characterize linker histone H1 proteoforms and their post-translational modifications (PTMs). This technique efficiently identifies H1 variants and their PTMs, advancing chromatin research.

Keywords:
Bottom-upChromatin remodelingEADFT-ICR MSLinker histonesPost-translational modificationsProteoformTIMSTop-downUVPDde novo sequencing

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Area of Science:

  • Proteomics
  • Chromatin Biology
  • Mass Spectrometry

Background:

  • Linker H1 histones are crucial for chromatin structure and gene regulation.
  • Post-translational modifications (PTMs) significantly influence H1 histone function.
  • Direct characterization of H1 proteoforms and their PTMs remains challenging.

Purpose of the Study:

  • To develop and validate a direct mass spectrometry-based method for characterizing linker H1 histone proteoforms.
  • To identify and map various PTMs on H1 histone variants.
  • To enable comprehensive analysis of H1 proteoform heterogeneity.

Main Methods:

  • Trapped ion mobility spectrometry coupled with UV photodissociation and Fourier transform ion cyclotron mass spectrometry (TIMS-q-UVPD-FT-ICR MS/MS).
  • Preseparation of proteoforms based on mobility and mass before fragmentation.
  • High mass accuracy detection of fragment ions for PTM assignment.
  • Complementary top-down (LC-q-EAD-ToF MS/MS) and bottom-up analyses for validation.

Main Results:

  • Direct characterization of four bovine H1 variants (H1.2, H1.3, H1.5, H1.4V) and their PTMs.
  • High sequence coverages (up to 60%) achieved for identified H1 proteoforms.
  • Identification of various PTMs including mono/dimethylation, acetylation, and phosphorylation.
  • De novo sequencing successfully identified the H1.4V variant sequence.

Conclusions:

  • The TIMS-q-UVPD-FT-ICR MS/MS method provides direct and efficient characterization of H1 proteoforms and their PTMs.
  • This approach requires minimal sample preparation and offers extensive PTM observation.
  • The method holds significant promise for global H1 proteoform analysis in chromatin research.