ArticleACS chemical biology2011
Caught in the act: covalent cross-linking captures activator-coactivator interactions in vivo.
Article in ACS chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 55 citations in OpenAlex.
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- Structural Robustness Affects the Engineerability of Aminoacyl-tRNA Synthetases for Genetic Code Expansion.Biochemistry · 2021Article
- Unexpected specificity within dynamic transcriptional protein-protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Two-step mechanism of J-domain action in driving Hsp70 function.PLoS computational biology · 2020Article
- Selective covalent capture of a DNA sequence corresponding to a cancer-driving C>G mutation in theRSC advances · 2019Article
- Electron-deficient p-benzoyl-l-phenylalanine derivatives increase covalent chemical capture yields for protein-protein interactions.Protein science : a publication of the Protein Society · 2019Article
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- Complementary Benzophenone Cross-Linking/Mass Spectrometry Photochemistry.Analytical chemistry · 2017Article
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- Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.Nature structural & molecular biology · 2016Article
- Discovery of Enzymatic Targets of Transcriptional Activators via in Vivo Covalent Chemical Capture.Journal of the American Chemical Society · 2016Article
- TRIC: Capturing the direct cellular targets of promoter-bound transcriptional activators.Protein science : a publication of the Protein Society · 2016Article
- Targeting transcription is no longer a quixotic quest.Nature chemical biology · 2015Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Currently there are few methods suitable for the discovery and characterization of transient, moderate affinity protein-protein interactions in their native environment, despite their prominent role in a host of cellular functions including protein folding, signal transduction, and transcriptional activation. Here we demonstrate that a genetically encoded photoactivatable amino acid, p-benzoyl-l-phenylalanine, can be used to capture transient and/or low affinity binding partners in an in vivo setting. In this study, we focused on ensnaring the coactivator binding partners of the transcriptional activator VP16 in S. cerevisiae. The interactions between transcriptional activators and coactivators in eukaryotes are moderate in affinity and short-lived, and due in part to these characteristics, identification of the direct binding partners of activators in vivo has met with only limited success. We find through in vivo photo-cross-linking that VP16 contacts the Swi/Snf chromatin-remodeling complex through the ATPase Snf2(BRG1/BRM) and the subunit Snf5 with two distinct regions of the activation domain. An analogous experiment with Gal4 reveals that Snf2 is also a target of this activator. These results suggest that Snf2 may be a valuable target for small molecule probe discovery given the prominent role the Swi/Snf complex family plays in development and in disease. More significantly, the successful implementation of the in vivo cross-linking methodology in this setting demonstrates that it can be applied to the discovery and characterization of a broad range of transient and/or modest affinity protein-protein interactions.
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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.