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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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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.
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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 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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Histone modification cross-talk and protein complex diversification confer plasticity to Polycomb repression.

Jacques Bonnet1, Eva Triantopoulou2, Jasmin Birnhäupl2

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Polycomb repressive complexes (PRCs) sculpt chromatin domains. Variant PRC1 and PRC2 complexes establish H2Aub1 and H3K27me3 marks, respectively, with PR-DUB counteracting these. Feedback loops ensure developmental stability.

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L(3)73AhPCGF proteinsPR-DUBPRC1PRC2Psc

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Area of Science:

  • Developmental Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Polycomb chromatin domains, marked by H2Aub1 and H3K27me3, regulate gene expression during development.
  • Polycomb group (PcG) protein complexes dynamically shape these domains.

Purpose of the Study:

  • To investigate the distinct roles of PcG subcomplexes in establishing H2Aub1 and H3K27me3 profiles in Drosophila embryos.
  • To understand the interplay between PcG complexes and histone modification cross-talk.

Main Methods:

  • Utilized Drosophila mutants lacking specific PcG complex functions.
  • Analyzed genome-wide histone modification patterns (H2Aub1 and H3K27me3).

Main Results:

  • Variant PRC1 generates bulk H2Aub1, while canonical PRC1 acts at target genes.
  • PR-DUB deubiquitinase removes H2Aub1 genome-wide.
  • PRC2.1 and PRC2.2 cooperate for H3K27me3 domain formation, with PRC2.1 limiting at HOX genes.
  • Loss of PRC2.1 function is partially rescued by loss of PR-DUB due to compensatory H2Aub1 accumulation and PRC2.2 activity.

Conclusions:

  • PcG complex diversification and feedback mechanisms provide robustness to developmental gene regulation.
  • Histone modification cross-talk allows for adaptability and buffering to maintain cell fate decisions.