ArticleThe Journal of cell biology1999
The RNA-editing enzyme ADAR1 is localized to the nascent ribonucleoprotein matrix on Xenopus lampbrush chromosomes but specifically associates with an atypical loop.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Recent Investigations on Neurotransmitters' Role in Acute White Matter Injury of Perinatal Glia and Pharmacotherapies-Glia Dynamics in Stem Cell Therapy.Molecular neurobiology · 2022Review
- Imaging the dynamics of transcription loops in living chromosomes.Chromosoma · 2018Article
- Unraveling molecular effects of ADAR1 overexpression in HEK293T cells by label-free quantitative proteomics.Cell cycle (Georgetown, Tex.) · 2016Article
- Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis.RNA (New York, N.Y.) · 2015Article
- Nascent-seq indicates widespread cotranscriptional RNA editing in Drosophila.Molecular cell · 2012Article
- Regulation of glutamate receptor B pre-mRNA splicing by RNA editing.Nucleic acids research · 2007Article
- Localized co-transcriptional recruitment of the multifunctional RNA-binding protein CELF1 by lampbrush chromosome transcription units.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2007Article
- ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing.Molecular and cellular biology · 2005Article
- Chromosomal storage of the RNA-editing enzyme ADAR1 in Xenopus oocytes.Molecular biology of the cell · 2005Article
- Effects of length and location on the cellular response to double-stranded RNA.Microbiology and molecular biology reviews : MMBR · 2004Review
- Distinct in vivo roles for double-stranded RNA-binding domains of the Xenopus RNA-editing enzyme ADAR1 in chromosomal targeting.The Journal of cell biology · 2003Article
- Precise identification of chicken chromosomes in the lampbrush form using chromosome painting probes.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2003Article
- Lampbrush chromosomes of the chaffinch (Fringilla coelebs L.).Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2003Article
- Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain.Molecular biology of the cell · 2002Article
- Lampbrush chromosomes and associated bodies: new insights into principles of nuclear structure and function.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2002Review
- CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain.Molecular and cellular biology · 2001Article
- The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein.Molecular biology of the cell · 2001Article
- RNA editing activity is associated with splicing factors in lnRNP particles: The nuclear pre-mRNA processing machinery.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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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
Double-stranded RNA adenosine deaminase (ADAR1, dsRAD, DRADA) converts adenosines to inosines in double-stranded RNAs. Few candidate substrates for ADAR1 editing are known at this point and it is not known how substrate recognition is achieved. In some cases editing sites are defined by basepaired regions formed between intronic and exonic sequences, suggesting that the enzyme might function cotranscriptionally. We have isolated two variants of Xenopus laevis ADAR1 for which no editing substrates are currently known. We demonstrate that both variants of the enzyme are associated with transcriptionally active chromosome loops suggesting that the enzyme acts cotranscriptionally. The widespread distribution of the protein along the entire chromosome indicates that ADAR1 associates with the RNP matrix in a substrate-independent manner. Inhibition of splicing, another cotranscriptional process, does not affect the chromosomal localization of ADAR1. Furthermore, we can show that the enzyme is dramatically enriched on a special RNA-containing loop that seems transcriptionally silent. Detailed analysis of this loop suggests that it might represent a site of ADAR1 storage or a site where active RNA editing is taking place. Finally, mutational analysis of ADAR1 demonstrates that a putative Z-DNA binding domain present in ADAR1 is not required for chromosomal targeting of the protein.
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