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Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis

ADAR (adenosine deaminase acting on RNA) is an RNA-editing enzyme present in most metazoans that converts adenosines in double-stranded RNA targets into inosines. Although the RNA targets of ADAR-mediated editing have been extensively cataloged, our understanding of the cellular function of such edi...

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Autores principales: Schweidenback, Caterina T.H., Emerman, Amy B., Jambhekar, Ashwini, Blower, Michael D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4338354/
https://www.ncbi.nlm.nih.gov/pubmed/25519486
http://dx.doi.org/10.1261/rna.047787.114
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author Schweidenback, Caterina T.H.
Emerman, Amy B.
Jambhekar, Ashwini
Blower, Michael D.
author_facet Schweidenback, Caterina T.H.
Emerman, Amy B.
Jambhekar, Ashwini
Blower, Michael D.
author_sort Schweidenback, Caterina T.H.
collection PubMed
description ADAR (adenosine deaminase acting on RNA) is an RNA-editing enzyme present in most metazoans that converts adenosines in double-stranded RNA targets into inosines. Although the RNA targets of ADAR-mediated editing have been extensively cataloged, our understanding of the cellular function of such editing remains incomplete. We report that long, double-stranded RNA added to Xenopus laevis egg extract is incorporated into an ADAR-containing complex whose protein components resemble those of stress granules. This complex localizes to microtubules, as assayed by accumulation on meiotic spindles. We observe that the length of a double-stranded RNA influences its incorporation into the microtubule-localized complex. ADAR forms a similar complex with endogenous RNA, but the endogenous complex fails to localize to microtubules. In addition, we characterize the endogenous, ADAR-associated RNAs and discover that they are enriched for transcripts encoding transcriptional regulators, zinc-finger proteins, and components of the secretory pathway. Interestingly, association with ADAR correlates with previously reported translational repression in early embryonic development. This work demonstrates that ADAR is a component of two, distinct ribonucleoprotein complexes that contain different types of RNAs and exhibit diverse cellular localization patterns. Our findings offer new insight into the potential cellular functions of ADAR.
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spelling pubmed-43383542016-02-01 Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis Schweidenback, Caterina T.H. Emerman, Amy B. Jambhekar, Ashwini Blower, Michael D. RNA Articles ADAR (adenosine deaminase acting on RNA) is an RNA-editing enzyme present in most metazoans that converts adenosines in double-stranded RNA targets into inosines. Although the RNA targets of ADAR-mediated editing have been extensively cataloged, our understanding of the cellular function of such editing remains incomplete. We report that long, double-stranded RNA added to Xenopus laevis egg extract is incorporated into an ADAR-containing complex whose protein components resemble those of stress granules. This complex localizes to microtubules, as assayed by accumulation on meiotic spindles. We observe that the length of a double-stranded RNA influences its incorporation into the microtubule-localized complex. ADAR forms a similar complex with endogenous RNA, but the endogenous complex fails to localize to microtubules. In addition, we characterize the endogenous, ADAR-associated RNAs and discover that they are enriched for transcripts encoding transcriptional regulators, zinc-finger proteins, and components of the secretory pathway. Interestingly, association with ADAR correlates with previously reported translational repression in early embryonic development. This work demonstrates that ADAR is a component of two, distinct ribonucleoprotein complexes that contain different types of RNAs and exhibit diverse cellular localization patterns. Our findings offer new insight into the potential cellular functions of ADAR. Cold Spring Harbor Laboratory Press 2015-02 /pmc/articles/PMC4338354/ /pubmed/25519486 http://dx.doi.org/10.1261/rna.047787.114 Text en © 2015 Schweidenback et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
spellingShingle Articles
Schweidenback, Caterina T.H.
Emerman, Amy B.
Jambhekar, Ashwini
Blower, Michael D.
Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis
title Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis
title_full Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis
title_fullStr Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis
title_full_unstemmed Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis
title_short Evidence for multiple, distinct ADAR-containing complexes in Xenopus laevis
title_sort evidence for multiple, distinct adar-containing complexes in xenopus laevis
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4338354/
https://www.ncbi.nlm.nih.gov/pubmed/25519486
http://dx.doi.org/10.1261/rna.047787.114
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