Dynamic response of RNA editing to temperature in Drosophila

Adenosine-to-inosine RNA editing is a highly conserved process that post-transcriptionally modifies mRNA, generating proteomic diversity, particularly within the nervous system of metazoans. Transcripts encoding proteins involved in neurotransmission predominate as targets of such modifications. Pre...

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Veröffentlicht in:BMC biology 2015-01, Vol.13 (1), p.1-1, Article 1
Hauptverfasser: Rieder, Leila E, Savva, Yiannis A, Reyna, Matthew A, Chang, Yao-Jen, Dorsky, Jacquelyn S, Rezaei, Ali, Reenan, Robert A
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container_issue 1
container_start_page 1
container_title BMC biology
container_volume 13
creator Rieder, Leila E
Savva, Yiannis A
Reyna, Matthew A
Chang, Yao-Jen
Dorsky, Jacquelyn S
Rezaei, Ali
Reenan, Robert A
description Adenosine-to-inosine RNA editing is a highly conserved process that post-transcriptionally modifies mRNA, generating proteomic diversity, particularly within the nervous system of metazoans. Transcripts encoding proteins involved in neurotransmission predominate as targets of such modifications. Previous reports suggest that RNA editing is responsive to environmental inputs in the form of temperature alterations. However, the molecular determinants underlying temperature-dependent RNA editing responses are not well understood. Using the poikilotherm Drosophila, we show that acute temperature alterations within a normal physiological range result in substantial changes in RNA editing levels. Our examination of particular sites reveals diversity in the patterns with which editing responds to temperature, and these patterns are conserved across five species of Drosophilidae representing over 10 million years of divergence. In addition, we show that expression of the editing enzyme, ADAR (adenosine deaminase acting on RNA), is dramatically decreased at elevated temperatures, partially, but not fully, explaining some target responses to temperature. Interestingly, this reduction in editing enzyme levels at elevated temperature is only partially reversed by a return to lower temperatures. Lastly, we show that engineered structural variants of the most temperature-sensitive editing site, in a sodium channel transcript, perturb thermal responsiveness in RNA editing profile for a particular RNA structure. Our results suggest that the RNA editing process responds to temperature alterations via two distinct molecular mechanisms: through intrinsic thermo-sensitivity of the RNA structures that direct editing, and due to temperature sensitive expression or stability of the RNA editing enzyme. Environmental cues, in this case temperature, rapidly reprogram the Drosophila transcriptome through RNA editing, presumably resulting in altered proteomic ratios of edited and unedited proteins.
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Interestingly, this reduction in editing enzyme levels at elevated temperature is only partially reversed by a return to lower temperatures. Lastly, we show that engineered structural variants of the most temperature-sensitive editing site, in a sodium channel transcript, perturb thermal responsiveness in RNA editing profile for a particular RNA structure. Our results suggest that the RNA editing process responds to temperature alterations via two distinct molecular mechanisms: through intrinsic thermo-sensitivity of the RNA structures that direct editing, and due to temperature sensitive expression or stability of the RNA editing enzyme. 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subjects Adenosine Deaminase - metabolism
Analysis
Animals
Conserved Sequence
Drosophila
Drosophila melanogaster - genetics
Drosophila Proteins - metabolism
Drosophilidae
Enzymes
Genetic aspects
Genetic transcription
Messenger RNA
Metazoa
Models, Molecular
Mutation - genetics
Physiological aspects
Protein Isoforms - genetics
RNA Editing - genetics
Temperature
Wildlife conservation
title Dynamic response of RNA editing to temperature in Drosophila
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