ArticleMolecular & cellular proteomics : MCP2016
A Quantitative Proteomic Analysis of In Vitro Assembled Chromatin.
Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- DNA mimic foldamers affect chromatin composition and disturb cell cycle progression.Nucleic acids research · 2023Article
- Cell-free genomics reveal intrinsic, cooperative and competitive determinants of chromatin interactions.Nucleic acids research · 2021Article
- Nucleosome Assembly and DisassemblyFrontiers in cell and developmental biology · 2021Article
- A Drosophila cell-free system that senses DNA breaks and triggers phosphorylation signalling.Nucleic acids research · 2019Article
- Data on the kinetics of in vitro assembled chromatin.Data in brief · 2016Article
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Authors and funding
6 authors.
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Abstract
The structure of chromatin is critical for many aspects of cellular physiology and is considered to be the primary medium to store epigenetic information. It is defined by the histone molecules that constitute the nucleosome, the positioning of the nucleosomes along the DNA and the non-histone proteins that associate with it. These factors help to establish and maintain a largely DNA sequence-independent but surprisingly stable structure. Chromatin is extensively disassembled and reassembled during DNA replication, repair, recombination or transcription in order to allow the necessary factors to gain access to their substrate. Despite such constant interference with chromatin structure, the epigenetic information is generally well maintained. Surprisingly, the mechanisms that coordinate chromatin assembly and ensure proper assembly are not particularly well understood. Here, we use label free quantitative mass spectrometry to describe the kinetics of in vitro assembled chromatin supported by an embryo extract prepared from preblastoderm Drosophila melanogaster embryos. The use of a data independent acquisition method for proteome wide quantitation allows a time resolved comparison of in vitro chromatin assembly. A comparison of our in vitro data with proteomic studies of replicative chromatin assembly in vivo reveals an extensive overlap showing that the in vitro system can be used for investigating the kinetics of chromatin assembly in a proteome-wide manner.
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