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Related Concept Videos

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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Nucleosome Remodeling02:54

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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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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 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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Position-effect Variegation02:32

Position-effect Variegation

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In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
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Heterochromatin02:38

Heterochromatin

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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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Updated: Sep 27, 2025

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis
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Multivalent DNA and nucleosome acidic patch interactions specify VRK1 mitotic localization and activity.

Gabrielle R Budziszewski1, Yani Zhao2, Cathy J Spangler1

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Vaccinia-related kinase 1 (VRK1) binds DNA and nucleosomes to phosphorylate histone H3. Mutations in VRK1

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Chromatin kinases regulate cell division by phosphorylating histone tails during mitosis.
  • Vaccinia-related kinase 1 (VRK1) phosphorylates histone H3 threonine 3 (H3T3) and other chromatin targets.
  • Mechanisms of kinase interaction with chromatin remain largely undefined.

Purpose of the Study:

  • To elucidate the mechanism of VRK1 chromatin engagement.
  • To investigate the role of VRK1 in H3T3 phosphorylation.
  • To explore the molecular basis of VRK1-associated spinal muscular atrophy.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine structural interactions.
  • Biochemical assays to assess binding affinities and enzymatic activity.
  • Cellular assays to evaluate VRK1 localization and function during mitosis.

Main Results:

  • VRK1 interacts with both linker DNA and the nucleosome acidic patch.
  • An arginine-rich C-terminal tail mediates VRK1 binding to the acidic patch.
  • Mutations in the VRK1 acidic patch motif cause adult-onset distal spinal muscular atrophy by disrupting nucleosome binding.
  • VRK1 mutations lead to mislocalization during mitosis, revealing a pathogenic mechanism.

Conclusions:

  • VRK1 utilizes both DNA and nucleosome acidic patch interactions for chromatin binding.
  • The C-terminal tail is crucial for VRK1-nucleosome interaction and H3T3 phosphorylation.
  • Dysfunctional VRK1-nucleosome binding due to mutations in the acidic patch motif underlies spinal muscular atrophy pathogenesis.