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Abstract
Adenosine to inosine (A-to-I) RNA editing is a highly conserved regulatory process carried out by adenosine-deaminases (ADARs) on double-stranded RNA (dsRNAs). Although a considerable fraction of the transcriptome is edited, the function of most editing sites is unknown. Previous studies indicate changes in A-to-I RNA editing frequencies following exposure to several stress types. However, the overall effect of stress on the expression of ADAR targets is not fully understood. Here, we performed high-throughput RNA sequencing of wild-type and ADAR mutant Caenorhabditis elegans worms after heat-shock to analyze the effect of heat-shock stress on the expression pattern of genes. We found that ADAR regulation following heat-shock does not directly involve heat-shock related genes. Our analysis also revealed that long non-coding RNAs (lncRNAs) and pseudogenes, which have a tendency for secondary RNA structures, are enriched among upregulated genes following heat-shock in ADAR mutant worms. The same group of genes is downregulated in ADAR mutant worms under permissive conditions, which is likely, considering that A-to-I editing protects endogenous dsRNA from RNA-interference (RNAi). Therefore, temperature increases may destabilize dsRNA structures and protect them from RNAi degradation, despite the lack of ADAR function. These findings shed new light on the dynamics of gene expression under heat-shock in relation to ADAR function.
Highlights
The survival of an organism depends on its ability to cope with environmental stresses
Consistent with our previous data for L4 developmental stage [17], the expression of 3’untranslated regions (UTRs) edited genes was reduced in relation to all genes in ADAR mutant worms compared to the wild-type (p-value = 3.4 × 10−7, Welch two-sample T-test) (Figure 2A)
We sought to gain insight into the roles of Adenosine to inosine (A-to-I) RNA editing in C. elegans adaptation to heat stress
Summary
The survival of an organism depends on its ability to cope with environmental stresses. Oxidants, and heavy metals results in protein misfolding and aggregation, leading to protein homeostasis (proteostasis) disruptions. To counteract these detrimental effects, organisms initiate heat-shock response (HSR), an ancient mechanism, conserved from archaebacteria to mammals [1,2]. HSR is not cell-autonomous, but rather regulated by neuronal and endocrine pathways. This is done to integrate the response with other organismal processes
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