ArticleJournal of proteomics2014
Incorporating DNA shearing in standard affinity purification allows simultaneous identification of both soluble and chromatin-bound interaction partners.
Article in Journal of proteomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- High-Efficiency Enrichment by Saturating Nanoliters of Protein Affinity Media.Analytical chemistry · 2023Article
- The MITF regulatory network in melanoma.Pigment cell & melanoma research · 2022Article
- A Nutrient-Based Cellular Model to Characterize Acetylation-Dependent Protein-Protein Interactions.Frontiers in molecular biosciences · 2022Article
- TBX2 controls a proproliferative gene expression program in melanoma.Genes & development · 2021Article
- Identification of covalent modifications regulating immune signaling complex composition and phenotype.Molecular systems biology · 2021Article
- BRN2 suppresses apoptosis, reprograms DNA damage repair, and is associated with a high somatic mutation burden in melanoma.Genes & development · 2019Article
- Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains.Molecular cell · 2019Article
- Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.Molecular & cellular proteomics : MCP · 2018Article
- Agonist-specific Protein Interactomes of Glucocorticoid and Androgen Receptor as Revealed by Proximity Mapping.Molecular & cellular proteomics : MCP · 2017Article
- Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling.Journal of visualized experiments : JoVE · 2017Article
- The Composition of the Arabidopsis RNA Polymerase II Transcript Elongation Complex Reveals the Interplay between Elongation and mRNA Processing Factors.The Plant cell · 2017Article
- Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma Cells.Cell chemical biology · 2017Article
- Assessing histone demethylase inhibitors in cells: lessons learned.Epigenetics & chromatin · 2017Article
- Multivalent Histone and DNA Engagement by a PHD/BRD/PWWP Triple Reader Cassette Recruits ZMYND8 to K14ac-Rich Chromatin.Cell reports · 2016Article
- Meet the neighbors: Mapping local protein interactomes by proximity-dependent labeling with BioID.Proteomics · 2016Review
- Proximity biotinylation and affinity purification are complementary approaches for the interactome mapping of chromatin-associated protein complexes.Journal of proteomics · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Affinity purification coupled to mass spectrometry (AP-MS) is an effective means of identifying protein-protein interactions to better understand biological functions. However, issues associated with sample preparation still limit the success of AP-MS for specific classes of proteins, including those associated with chromatin that exhibit overall poor solubility in the protocols normally used for AP-MS analysis. Here, we wanted to provide a generally applicable method to simultaneously identify interactors for the chromatin-bound and the soluble fractions of a given bait protein. Using four FLAG-tagged canonical histone proteins (H2A, H2B, H3.1 and H4) we demonstrate that the chromatin solubility issue can be robustly alleviated by fragmenting DNA prior to AP-MS using a combination of sonication and nuclease treatment. We show that - in comparison to a commonly used AP-MS method - our optimized protocol greatly improves the recovery of chromatin-associated interactors for core histones. Critically, this is achieved while preserving the interaction partners associated with the soluble portion of the histones. Detailed protocols amenable to the study of both histone and non-histone baits are presented here. BIOLOGICAL SIGNIFICANCE: This manuscript describes workflow improvements to enable the recovery of chromatin-bound interactors by affinity purification coupled to mass spectrometry (AP-MS). This is significant, as most of the high-throughput studies to date can only monitor protein-protein interactions for soluble (not bound to chromatin) components. By consequence, we still poorly understand how protein complexes form on chromatin, which greatly hampers our understanding of gene expression. Using core histones as test cases, we show here a simple and universally applicable workflow that permits the identification of chromatin-bound protein-protein interactions. As exemplified in our manuscript, this revised protocol should result in a much deeper understanding of chromatin biology. This article is part of a Special Issue: Can Proteomics Fill the Gap Between Genomics and Phenotypes?
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.