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Article
Mechanistic insights into histone deposition and nucleosome assembly by the chromatin assembly factor-1.
Public Deposited
https://scholar.colorado.edu/concern/articles/fb494886q
- Abstract
- Eukaryotic chromatin is a highly dynamic structure with essential roles in virtually all DNA-dependent cellular processes. Nucleosomes are a barrier to DNA access, and during DNA replication, they are disassembled ahead of the replication machinery (the replisome) and reassembled following its passage. The Histone chaperone Chromatin Assembly Factor-1 (CAF-1) interacts with the replisome and deposits H3-H4 directly onto newly synthesized DNA. Therefore, CAF-1 is important for the establishment and propagation of chromatin structure. The molecular mechanism by which CAF-1 mediates H3-H4 deposition has remained unclear. However, recent studies have revealed new insights into the architecture and stoichiometry of the trimeric CAF-1 complex and how it interacts with and deposits H3-H4 onto substrate DNA. The CAF-1 trimer binds to a single H3-H4 dimer, which induces a conformational rearrangement in CAF-1 promoting its interaction with substrate DNA. Two CAF-1•H3-H4 complexes co-associate on nucleosome-free DNA depositing (H3-H4)2 tetramers in the first step of nucleosome assembly. Here, we review the progress made in our understanding of CAF-1 structure, mechanism of action, and how CAF-1 contributes to chromatin dynamics during DNA replication.
- Creator
- Date Issued
- 2018-11-02
- Academic Affiliation
- Journal Title
- Journal Issue/Number
- 19
- Journal Volume
- 46
- File Extent
- 9907-9917
- Publisher
- Last Modified
- 2019-12-05
- Identifier
- PubMed ID: 30239791
- Resource Type
- Rights Statement
- License
- DOI
- ISSN
- 1362-4962
- Language
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mechanisticInsightsIntoHistoneDepositionAndNucleosomeAssem.pdf | 2019-12-05 | Public | Download |