ArticleNuclear receptor signaling2010
DamIP: a novel method to identify DNA binding sites in vivo.
Article in Nuclear receptor signaling, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- DNA NPlants (Basel, Switzerland) · 2020Review
- Dam mutants provide improved sensitivity and spatial resolution for profiling transcription factor binding.Epigenetics & chromatin · 2019Article
- DamID as a versatile tool for understanding gene regulation.Development (Cambridge, England) · 2019Review
- MadID, a Versatile Approach to Map Protein-DNA Interactions, Highlights Telomere-Nuclear Envelope Contact Sites in Human Cells.Cell reports · 2018Article
- CATaDa reveals global remodelling of chromatin accessibility during stem cell differentiation in vivo.eLife · 2018Article
- Human MAF1 targets and represses active RNA polymerase III genes by preventing recruitment rather than inducing long-term transcriptional arrest.Genome research · 2016Article
- Getting Down to Specifics: Profiling Gene Expression and Protein-DNA Interactions in a Cell Type-Specific Manner.Advances in genetics · 2015Review
- DNA Methylation.EcoSal Plus · 2014Article
- Interpreting the regulatory genome: the genomics of transcription factor function in Drosophila melanogaster.Briefings in functional genomics · 2012Article
- Research resource: The estrogen receptor α cistrome defined by DamIP.Molecular endocrinology (Baltimore, Md.) · 2012Article
- DamIP: using mutant DNA adenine methyltransferase to study DNA-protein interactions in vivo.Current protocols in molecular biology · 2011Article
- Dam it's good! DamID profiling of protein-DNA interactions.Wiley interdisciplinary reviews. Developmental biologyReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Identifying binding sites and target genes of transcription factors is a major biologic problem. The most commonly used current technique, chromatin immunoprecipitation (ChIP), is dependent on a high quality antibody for each protein of interest, which is not always available, and is also cumbersome, involving sequential cross-linking and reversal of cross-linking. We have developed a novel strategy to study protein DNA binding sites in vivo, which we term DamIP. By tethering a mutant form of E. coli DNA adenine methyltransferase to the target protein, the fusion protein introduces N-6-adenosine methylation to sequences proximal to the protein binding sites. DNA fragments with this modification, which is absent in eukaryotes, are detected using an antibody directed against methylated adenosine. For an initial test of the method we used human estrogen receptor alpha (hERalpha), one of the best studied transcription factors. We found that expression of Dam-hERalpha fusion proteins in MCF-7 cells introduces adenosine methylation near a series of known direct hERalpha binding sites. Specific methylation tags are also found at indirect hERalpha binding sites, including both primary binding sites for the ER interactors AP-1 and SP1, and promoters that are activated by upstream ER bound enhancers. DamIP provides a new tool for the study of DNA interacting protein function in vivo.
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Registered trials
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.