ArticleThe EMBO journal2002
The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 69 citations in OpenAlex.
- Article
- Arid5a uses disordered extensions of its core ARID domain for distinct DNA- and RNA-recognition and gene regulation.The Journal of biological chemistry · 2024Article
- ARID3a from the ARID family: structure, role in autoimmune diseases and drug discovery.Acta pharmacologica Sinica · 2023Review
- Cell context-dependent CFI-1/ARID3 functions control neuronal terminal differentiation.Cell reports · 2023Article
- Conservation and Expansion of Transcriptional Factor Repertoire in theJournal of fungi (Basel, Switzerland) · 2023Article
- Conservation and Expansion of Transcriptional Factor Repertoire in thebioRxiv : the preprint server for biology · 2023Article
- DNA binding by polycomb-group proteins: searching for the link to CpG islands.Nucleic acids research · 2022Review
- Missense Variants Reveal Functional Insights Into the Human ARID Family of Gene Regulators.Journal of molecular biology · 2022Article
- Structure and DNA binding analysis of AT-rich interaction domain present in human BAF-B specific subunit BAF250b.Protein science : a publication of the Protein Society · 2022Article
- In vivo vaccination with cell line-derived whole tumor lysates: neoantigen quality, not quantity matters.Journal of translational medicine · 2020Article
- Dual Recognition of H3K4me3 and DNA by the ISWI Component ARID5 Regulates the Floral Transition in Arabidopsis.The Plant cell · 2020Article
- Deciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana.Plant molecular biology · 2016Article
- An inhibitor of KDM5 demethylases reduces survival of drug-tolerant cancer cells.Nature chemical biology · 2016Article
- Mutations in the KDM5C ARID Domain and Their Plausible Association with Syndromic Claes-Jensen-Type Disease.International journal of molecular sciences · 2015Article
- Binding of human SWI1 ARID domain to DNA without sequence specificity: A molecular dynamics study.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2015Article
- Communication routes in ARID domains between distal residues in helix 5 and the DNA-binding loops.PLoS computational biology · 2014Article
- ARID1a-DNA interactions are required for promoter occupancy by SWI/SNF.Molecular and cellular biology · 2013Article
- Plant proteins containing high mobility group box DNA-binding domains modulate different nuclear processes.Plant physiology · 2012Review
- Preparation and optimization of protein-DNA complexes suitable for detailed NMR studies.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Characterization of a new ARID family transcription factor (Brightlike/ARID3C) that co-activates Bright/ARID3A-mediated immunoglobulin gene transcription.Molecular immunology · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The AT-rich interaction domain (ARID) is a DNA-binding module found in many eukaryotic transcription factors. Using NMR spectroscopy, we have determined the first ever three-dimensional structure of an ARID--DNA complex (mol. wt 25.7 kDa) formed by Dead ringer from Drosophila melanogaster. ARIDs recognize DNA through a novel mechanism involving major groove immobilization of a large loop that connects the helices of a non-canonical helix-turn-helix motif, and through a concomitant structural rearrangement that produces stabilizing contacts from a beta-hairpin. Dead ringer's preference for AT-rich DNA originates from three positions within the ARID fold that form energetically significant contacts to an adenine-thymine base step. Amino acids that dictate binding specificity are not highly conserved, suggesting that ARIDs will bind to a range of nucleotide sequences. Extended ARIDs, found in several sequence-specific transcription factors, are distinguished by the presence of a C-terminal helix that may increase their intrinsic affinity for DNA. The prevalence of serine amino acids at all specificity determining positions suggests that ARIDs within SWI/SNF-related complexes will interact with DNA non-sequence specifically.
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