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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.
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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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The Nucleosome Core Particle02:10

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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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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 at the Centromere02:30

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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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Genome protection: histone H4 and beyond.

Kundan Kumar1,2, Romila Moirangthem1, Rupinder Kaur3

  • 1Laboratory of Fungal Pathogenesis, Centre for DNA Fingerprinting and Diagnostics (CDFD), Hyderabad, Telangana, 500039, India.

Current Genetics
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Reduced histone H4 gene dosage confers methyl methanesulfonate (MMS) resistance in Candida glabrata by enhancing homologous recombination (HR). This finding is crucial for understanding stress responses in this fungal pathogen.

Keywords:
ChromatinGenome integrityHistonesHomologous recombinationHuman fungal pathogensMethyl methanesulfonate (MMS)Stress resistance

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Area of Science:

  • Molecular Biology
  • Genetics
  • Mycology

Background:

  • Histone dosage impacts DNA accessibility and repair efficiency.
  • Surplus histones can hinder DNA repair, specifically homologous recombination (HR).
  • Candida glabrata is an opportunistic fungal pathogen with implications for human health.

Purpose of the Study:

  • To investigate the association between histone H4 gene dosage and methyl methanesulfonate (MMS) resistance in Candida glabrata.
  • To explore the role of homologous recombination (HR) in MMS resistance linked to reduced histone H4 levels.
  • To identify specific histone H4 residues involved in DNA repair and stress response.

Main Methods:

  • Genetic analysis of histone H4-encoding ORFs (CgHHF1, CgHHF2) in Candida glabrata.
  • Assessing methyl methanesulfonate (MMS) resistance in mutant strains.
  • Homologous recombination (HR) rate analysis.
  • Interactome analysis of histones H3 and H4.
  • Site-directed mutagenesis to investigate specific amino acid residues.

Main Results:

  • Reduced histone H4 gene dosage (Cghhf1Δhhf2Δ mutant) confers resistance to MMS-induced DNA damage.
  • This resistance is associated with an elevated rate of homologous recombination (HR).
  • An arginine residue at position 95 in histone H4's C-terminal tail is critical for complementing MMS resistance.

Conclusions:

  • Reduced histone H4 levels enhance DNA repair through homologous recombination (HR) in Candida glabrata, conferring MMS resistance.
  • Specific histone H4 residues, like R95, play a role in mediating DNA repair and stress resistance.
  • Histone H4 dosage modulation is a potential mechanism for stress adaptation in this pathogenic yeast.