Chromatin Proteomics
Chromatin Proteomics - Related Videos
08:11
Quantitative Analysis of Chromatin Proteomes in Disease
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Cited by 4 •
2012
Advances in mass spectrometry have allowed the high throughput analysis of protein expression and modification in a host of tissues. Combined with subcellular fractionation and disease models, quantitative mass spectrometry and bioinformatics can reveal new properties in biological systems. The method described herein analyzes chromatin-associated proteins in the setting of heart disease and is readily applicable to other in vivo models of human disease.
24:02
The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin
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Cited by 27 •
2014
By combining native and crosslinking chromatin immunoprecipitation with high-resolution Mass Spectrometry, ChroP approach enables to dissect the composite proteomic architecture of histone modifications, variants and non-histonic proteins synergizing at functionally distinct chromatin domains.
09:29
Skeletal Muscle Gender Dimorphism from Proteomics
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Cited by 4 •
2011
A straight-forward set of methods to isolate and determine the identity of the most abundant proteins expressed in skeletal muscle. About 800 spots are discerned on a two-dimensional gel from 10 mg muscle; this allows for the determination of gender-specific protein expression. These methods will give equivalent results in most tissues.
09:27
Adaptation of Hybridization Capture of Chromatin-associated Proteins for Proteomics to Mammalian Cells
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Cited by 2 •
2018
This is a method to identify novel DNA-interacting proteins at specific target loci, relying on sequence-specific capture of crosslinked chromatin for subsequent proteomic analyses. No prior knowledge about potential binding proteins, nor cell modifications are required. Initially developed for yeast, the technology has now been adapted for mammalian cells.
08:39
Chromatin Immunoprecipitation
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2023
Histones are proteins that help organize DNA in eukaryotic nuclei by serving as “scaffolds” around which DNA can be wrapped, forming a complex called “chromatin”. These proteins can be modified through the addition of chemical groups, and these changes affect gene expression. Researchers use a technique called chromatin immunoprecipitation (ChIP) to better understand which DNA regions associate with specific histone modifications or other gene regulatory proteins. Antibodies are used to isolate...
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Changes in the abundance of histones, transcription factors, chromatin remodelers, and regulatory post-translational modifications provide a molecular view of chromatin state. Comparing these protein patterns with biological conditions helps researchers connect chromatin composition to changes in gene regulation. This approach is especially useful when studying how cells alter genome organization during development, differentiation, disease, or environmental responses.
Post-translational modifications add regulatory information beyond protein abundance. Their patterns can indicate that chromatin-associated proteins have changed function or regulatory status under a particular biological condition. Measuring these modifications alongside histones and other chromatin proteins therefore helps distinguish a change in protein quantity from a broader alteration in chromatin regulation and genome organization.
Comparative profiles can show which chromatin proteins or modifications vary between developmental stages, differentiated and undifferentiated cells, disease states, or environmental treatments. These differences provide evidence for condition-associated changes in chromatin composition. Interpreting the protein and modification patterns together helps relate molecular changes in chromatin to cellular function and regulation of the genome.
The workflow begins by isolating chromatin from the biological sample. Its associated proteins are then enzymatically digested into peptides, which are separated by liquid chromatography and analyzed with tandem mass spectrometry. The resulting measurements support identification and quantification of chromatin-associated proteins and their modifications, allowing researchers to compare chromatin composition across samples or conditions.
Chromatin proteomics can measure several protein categories associated with genome organization, including histones, transcription factors, and chromatin remodelers. It can also characterize regulatory post-translational modifications on these proteins. Examining these components together gives a broader picture than assessing a single protein, because the data represent both structural and regulatory features of chromatin.
Researchers apply this method when they need to examine how chromatin changes across development, cell differentiation, disease, or responses to environmental signals. The approach can connect altered protein abundance and modification patterns with gene regulation and cellular function. Consequently, it supports investigations of epigenetic mechanisms and of how genome organization changes in biologically meaningful contexts.