ArticleThe Journal of cell biology2003
Distinct in vivo roles for double-stranded RNA-binding domains of the Xenopus RNA-editing enzyme ADAR1 in chromosomal targeting.
Article in The Journal of cell biology, 2003. 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, 25 citations in OpenAlex.
- ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024Review
- To protect and modify double-stranded RNA - the critical roles of ADARs in development, immunity and oncogenesis.Critical reviews in biochemistry and molecular biology · 2021Review
- Article
- A protein-protein interaction underlies the molecular basis for substrate recognition by an adenosine-to-inosine RNA-editing enzyme.Nucleic acids research · 2018Article
- Knockdown of ZFR suppresses cell proliferation and invasion of human pancreatic cancer.Biological research · 2016Article
- ATP-independent diffusion of double-stranded RNA binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A zipcode unzipped.Genes & development · 2012Article
- Synthesis and evaluation of an RNA editing substrate bearing 2'-deoxy-2'-mercaptoadenosine.Nucleosides, nucleotides & nucleic acids · 2009Article
- RNA aptamers binding the double-stranded RNA-binding domain.RNA (New York, N.Y.) · 2006Article
- ADAR2-mediated editing of RNA substrates in the nucleolus is inhibited by C/D small nucleolar RNAs.The Journal of cell biology · 2005Article
- Effects of length and location on the cellular response to double-stranded RNA.Microbiology and molecular biology reviews : MMBR · 2004Review
- Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA-editing enzyme adenosine deaminase that acts on RNA (ADAR1) deaminates adenosines to inosines in double-stranded RNA substrates. Currently, it is not clear how the enzyme targets and discriminates different substrates in vivo. However, it has been shown that the deaminase domain plays an important role in distinguishing various adenosines within a given substrate RNA in vitro. Previously, we could show that Xenopus ADAR1 is associated with nascent transcripts on transcriptionally active lampbrush chromosomes, indicating that initial substrate binding and possibly editing itself occurs cotranscriptionally. Here, we demonstrate that chromosomal association depends solely on the three double-stranded RNA-binding domains (dsRBDs) found in the central part of ADAR1, but not on the Z-DNA-binding domain in the NH2 terminus nor the catalytic deaminase domain in the COOH terminus of the protein. Most importantly, we show that individual dsRBDs are capable of recognizing different chromosomal sites in an apparently specific manner. Thus, our results not only prove the requirement of dsRBDs for chromosomal targeting, but also show that individual dsRBDs have distinct in vivo localization capabilities that may be important for initial substrate recognition and subsequent editing specificity.
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