Proteomics

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In vitro chromatin assembly - A quantitative proteomic analysis of in vitro assembled chromatin

ABSTRACT: Here, we use LC-MSMS and SWATH-MS to describe the kinetics of in vitro assembled chromatin supported by an embryo extract prepared from preblastoderm Drosophila melanogaster embryos. This system allows easy manipulation of distinct aspects of chromatin assembly such as post-translational histone modifications, the levels of histone chaperones and the concentration of distinct DNA binding factors. Our findings support the idea that chromatin assembly factors and factors important for chromatin structure bind chromatin an ordered manner, which is -at least in part- regulated by histone deacetylation.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

TISSUE(S): Embryo

SUBMITTER: Moritz Voelker-Albert  

LAB HEAD: Axel Imhof

PROVIDER: PXD003445 | Pride | 2016-01-27

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
1406016_OT1_IF_D_pDNA_4h_2.RAW Raw
140604_OT1_IF_10_pDNA_4h_2.RAW Raw
140604_OT1_IF_1_mDNA_1h_1.RAW Raw
140604_OT1_IF_2_mDNA_1h_2.RAW Raw
140604_OT1_IF_3_pDNA_1h_1.RAW Raw
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Publications

A Quantitative Proteomic Analysis of In Vitro Assembled Chromatin.

Völker-Albert Moritz Carl MC   Pusch Miriam Caroline MC   Fedisch Andreas A   Schilcher Pierre P   Schmidt Andreas A   Imhof Axel A  

Molecular & cellular proteomics : MCP 20160125 3

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 dur  ...[more]

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