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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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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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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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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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Histone Tails Promote PARP1-Dependent Structural Rearrangements in Nucleosomes.

N V Maluchenko1, D S Sultanov2, E Yu Kotova2

  • 1Moscow State University, 119234, Moscow, Russia. mal_nat@mail.ru.

Doklady. Biochemistry and Biophysics
|March 5, 2020
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Summary

Poly (ADP-ribose) polymerase 1 (PARP 1) changes nucleosome structure, affecting genome accessibility. Histone tails stabilize these PARP 1-induced changes without impacting PARP 1

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Poly (ADP-ribose) polymerase 1 (PARP 1) is a key enzyme involved in DNA repair and genome stability.
  • Nucleosomes, the basic units of DNA packaging, regulate access to genetic material.
  • The structural dynamics of nucleosomes are crucial for various cellular processes.

Purpose of the Study:

  • To investigate the role of histone tails in PARP 1-mediated nucleosome structural rearrangements.
  • To determine how histone tails influence the accessibility of genomic sites modulated by PARP 1.
  • To elucidate the interplay between histone tails, PARP 1 activity, and nucleosome structure.

Main Methods:

  • Chromatin immunoprecipitation (ChIP) assays to assess protein binding to DNA.
  • Nuclear magnetic resonance (NMR) spectroscopy to analyze nucleosome structural dynamics.
  • Enzyme activity assays to measure PARP 1 catalytic function.

Main Results:

  • PARP 1 binding induces significant alterations in nucleosomal DNA wrapping.
  • Non-structured histone tails are integral to facilitating and stabilizing PARP 1-induced nucleosome rearrangements.
  • Histone tails do not affect the enzymatic activity of PARP 1.

Conclusions:

  • Histone tails play a crucial structural role in PARP 1-mediated nucleosome modulation.
  • These findings highlight a novel mechanism by which histone tails influence genome accessibility.
  • Understanding this interaction is vital for comprehending DNA repair and gene regulation pathways.