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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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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 early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
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Epigenomic Modifications Mediating Antibody Maturation.

Emily C Sheppard1, Rikke Brandstrup Morrish1, Michael J Dillon1

  • 1Living Systems Institute, University of Exeter, Exeter, United Kingdom.

Frontiers in Immunology
|March 15, 2018
PubMed
Summary
This summary is machine-generated.

Epigenetic modifications regulate antibody maturation by controlling DNA repair at the immunoglobulin locus. Misregulation can lead to immunological disorders and cancer.

Keywords:
B cell maturationantibody diversityclass-switch recombinationcytosine deaminationepigenetic modificationsepigenomics and epigeneticssomatic hypermutation

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Area of Science:

  • Immunology
  • Epigenetics
  • Molecular Biology

Background:

  • Antibody maturation involves somatic hypermutation (SHM) and class-switch recombination (CSR).
  • Epigenetic modifications, including histone modifications, DNA methylation, and non-coding RNAs (ncRNA), play crucial roles in these processes.
  • Activation-Induced Cytidine Deaminase (AID) is a key enzyme that introduces DNA mutations during SHM and CSR.

Purpose of the Study:

  • To assess how distinct epigenetic modifications collectively influence DNA repair pathways at the immunoglobulin (Ig) locus.
  • To understand the mechanisms by which these modifications regulate AID recruitment and DNA repair factor stabilization.
  • To discuss the implications of epigenomic misregulation in antibody development, immunological syndromes, and cancer.

Main Methods:

  • Review and assessment of existing literature on epigenetic modifications and their roles in SHM and CSR.
  • Analysis of how histone modifications, DNA methylation, and ncRNAs interact to regulate the Ig locus.
  • Discussion of the downstream effects of these epigenetic mechanisms on DNA repair pathways.

Main Results:

  • Epigenetic modifications collectively orchestrate chromatin accessibility and recruit AID to the Ig locus.
  • Specific combinations of histone modifications, DNA methylation, and ncRNAs regulate AID activity and DNA repair.
  • These epigenetic mechanisms are critical for initiating differential DNA repair, leading to enhanced antibody affinity (SHM) or isotype switching (CSR).

Conclusions:

  • Epigenetic regulation is fundamental to achieving high-affinity antibodies and diverse antibody isotypes.
  • Dysregulation of these epigenetic processes can impair adaptive immunity and contribute to disease pathogenesis.
  • Targeting epigenetic mechanisms may offer therapeutic strategies for immunological disorders and cancers.