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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Spanning the gap: unraveling RSC dynamics in vivo.

Heinz Neumann1,2, Bryan J Wilkins3

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The yeast chromatin remodeler RSC binds to nucleosomes in living cells, with its interactions influenced by histone modifications like H2B SUMOylation and H3K14ac. RSC remains bound during mitosis, altering its binding mode throughout the cell cycle.

Keywords:
Chromatin remodellingGenetic code expansionLysine acetylationPhoto-crosslinkingRSCSumoylationUnnatural amino acids

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Area of Science:

  • Chromatin biology
  • Molecular mechanisms of gene regulation
  • Yeast genetics

Background:

  • The essential yeast chromatin remodeler, RSC, plays a critical role in nucleosome dynamics.
  • Previous studies provided structural analyses of RSC, but gaps remain in understanding subunit interactions and the impact of posttranslational modifications.
  • Histone modifications dynamically regulate remodeler binding and function, necessitating studies under physiological conditions.

Purpose of the Study:

  • To investigate the spatiotemporal binding of the RSC complex to nucleosomes in living yeast.
  • To elucidate the role of histone modifications in regulating RSC-nucleosome interactions.
  • To understand RSC binding dynamics during the cell cycle and mitosis.

Main Methods:

  • Utilized genetically encoded photo-activatable amino acids incorporated into histones in living yeast.
  • Monitored nucleosomal binding of RSC in vivo using these engineered histones.
  • Analyzed RSC binding preferences and alterations across different cell cycle stages and in response to histone modifications.

Main Results:

  • RSC preferentially binds to H2B SUMOylated nucleosomes in vivo.
  • RSC interacts with adjacent nucleosomes through H3K14ac.
  • RSC is constitutively bound to nucleosomes and is not ejected during mitotic chromatin compaction, with altered binding modes throughout the cell cycle.

Conclusions:

  • Histone modifications critically regulate RSC binding modes and function in a spatiotemporal manner.
  • RSC exhibits dynamic binding behavior to nucleosomes under physiological conditions, adapting to cell cycle progression.
  • This study provides a renewed perspective on RSC mechanics within the living nucleus.