Proteomics

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Examining the stability of nucleosomal modifications during pull-down affinity purification

ABSTRACT: Here we investigated the stability of nucleosomal modifications during pull-down affinity purification with HeLa nuclear extracts. Unmodified di-nucleosomes and di-nucleosomes decorated with H3K4me3K9acK14acK18acK23acK27ac, H4K5acK8acK12acK16acK20me2 and incorporating histone variant H2A.Z were incubated with HeLa nuclear extract or buffer alone for 4 hours at 4 degrees Celsius. The relative abundances of nucleosomal modifications were quantified using LC-MS.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Andrey Tvardovskiy  

LAB HEAD: Till Bartke

PROVIDER: PXD042823 | Pride | 2023-12-10

REPOSITORIES: Pride

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NPD_H3K4me3_9ac_H2A_Z_control_no_nuclear_extract_repl1.raw Raw
NPD_H3K4me3_9ac_H2A_Z_control_no_nuclear_extract_repl2.raw Raw
NPD_H3K4me3_9ac_H2A_Z_nuclear_extract_repl1.raw Raw
NPD_H3K4me3_9ac_H2A_Z_nuclear_extract_repl2.raw Raw
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Publications

DNA and histone modifications combine into characteristic patterns that demarcate functional regions of the genome<sup>1,2</sup>. While many 'readers' of individual modifications have been described<sup>3-5</sup>, how chromatin states comprising composite modification signatures, histone variants and internucleosomal linker DNA are interpreted is a major open question. Here we use a multidimensional proteomics strategy to systematically examine the interaction of around 2,000 nuclear proteins wi  ...[more]

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