Study : N6-methyladenosine and RNA secondary structure affect transcript stability and translation during systemic salt stress in Arabidopsis
Identification
Name
N6-methyladenosine and RNA secondary structure affect transcript stability and translation during systemic salt stress in Arabidopsis
Identifier
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Source
Description
After transcription, a messenger RNA (mRNA) is further post-transcriptionally regulated by several features including RNA secondary structure and covalent RNA modifications (specifically N6-methyladenosine, m6A). Both RNA secondary structure and m6A have been demonstrated to regulate mRNA stability and translation as well as have been independently linked to plant response to excess salt concentrations in the soil. However, the effect of m6A on regulating RNA secondary structure and the combinatorial interplay between these two RNA features during salt stress response has yet to be studied. Here, we globally identify RNA-protein interactions and RNA secondary structure during systemic salt stress. This analysis reveals that RNA secondary structure is highly dynamic during salt stress, which is independent of changes in RNA-protein interactions. Conversely, we find that m6A is anti-correlated with RNA secondary structure in a condition-specific manner, with salt-specific m6A resulting in a decrease in mRNA secondary structure during salt stress. Remarkably, we show that the combination of salt-specific m6A deposition and the associated loss of RNA secondary structure results in increases in mRNA stability and translation of transcripts encoding proteins involved in responses to abiotic stresses. In total, our comprehensive analyses reveal an important epitranscriptome, secondary structure-mediated post-transcriptional regulatory mechanism involved in plant long-term salt stress response and adaptation. Overall design: Protein interaction profile sequencing (PIP-seq_ in the nuclei of Arabidopsis thanliana rosette leaves treated with or without long term salt stress. These are crosslinked with formaldehyde and treated with two Rnases (ssRNase and dsRNase) in two biological replicates over three lanes of sequencing
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