Chromatin Proteome Analysis

Chromatin proteome analysis is the systematic identification and characterization of proteins associated with chromatin, the DNA–protein complex that organizes the genome and regulates gene activity. In this approach, chromatin is isolated from cells or tissues, associated proteins are extracted and separated, and mass spectrometry or related proteomic methods identify histones, transcription factors, chromatin remodelers, and post-translational modifications that influence DNA accessibility. In medicine, the method helps reveal how epigenetic regulation changes during development, cancer, inflammation, and drug response. Comparing chromatin protein profiles across conditions can identify disease-associated pathways, potential biomarkers, and therapeutic targets while clarifying mechanisms of altered gene expression.

Chromatin Proteome Analysis - Related Videos

Research

JoVE Journal - Medicine

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.

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.

Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes

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Cited by 20 •

2017

Sequential salt extraction of chromatin bound proteins is a useful tool for determining the binding properties of large protein complexes. This method can be employed to evaluate the role of individual subunits or domains in the overall affinity of a protein complex to bulk chromatin.

Research

JoVE Journal - Medicine
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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.

Analysis of the c-KIT Ligand Promoter Using Chromatin Immunoprecipitation

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2017

DNA-protein interactions are essential for multiple biological processes. During the evaluation of cellular functions, the analysis of DNA-protein interactions is indispensable for understanding gene regulation. Chromatin immunoprecipitation (ChIP) is a powerful tool to analyze such interactions in vivo.

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