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Related Concept Videos

Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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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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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The Nucleosome02:33

The Nucleosome

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DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
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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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The Nucleosome Core Particle

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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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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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Functional Assessment of BRCA1 variants using CRISPR-Mediated Base Editors
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BRCA1/BARD1 is a nucleosome reader and writer.

Samuel R Witus1, Weixing Zhao2, Peter S Brzovic1

  • 1Department of Biochemistry, University of Washington School of Medicine, Seattle, WA, USA.

Trends in Biochemical Sciences
|March 30, 2022
PubMed
Summary

Mutations in BRCA1 and BARD1 increase cancer risk. This review details how the BRCA1/BARD1 complex interacts with chromatin to regulate gene transcription and DNA repair, offering new insights into its cancer-associated functions.

Keywords:
DNA damage repairchromatin regulationhomologous recombinationtranscriptional regulationubiquitin ligase

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Area of Science:

  • Molecular Biology
  • Cancer Genetics
  • Structural Biology

Background:

  • Mutations in BRCA1 and BARD1 are linked to hereditary breast and ovarian cancers.
  • The BRCA1/BARD1 complex is a crucial regulator of transcription and DNA repair.
  • The precise mechanisms of BRCA1/BARD1 interaction with chromatin were previously unknown.

Purpose of the Study:

  • To review recent advancements in understanding BRCA1/BARD1's chromatin interactions.
  • To elucidate how BRCA1/BARD1 functions as a nucleosome reader and writer.
  • To connect these mechanisms to transcriptional regulation and DNA repair.

Main Methods:

  • Review of recent structural biology studies.
  • Analysis of cellular biology findings.
  • Integration of data on BRCA1/BARD1's enzymatic activity (E3 ubiquitin ligase).

Main Results:

  • BRCA1/BARD1 acts as both a "reader" and "writer" on nucleosomes.
  • These functions are critical for transcriptional regulation.
  • The complex plays a key role in DNA repair via homologous recombination.

Conclusions:

  • Recent structural and cellular biology insights clarify BRCA1/BARD1's chromatin interface.
  • Understanding these mechanisms is vital for comprehending BRCA1/BARD1's role in cancer predisposition.
  • This knowledge advances the study of gene regulation and genome stability.