Comparative genomic analyses reveal evidence for adaptive A-to-I RNA editing in insect Adar gene

Abstract

Although A-to-I RNA editing leads to similar effects to A-to-G DNA mutation, nonsynonymous RNA editing (recoding) is believed to confer its adaptiveness by ‘epigenetically’ regulating proteomic diversity in a temporospatial manner, avoiding the pleiotropic effect of genomic mutations. Recent discoveries on the evolutionary trajectory of Ser>Gly auto-editing site in insect Adar gene demonstrated a selective advantage to having an editable codon compared to uneditable ones. However, apart from pure observations, quantitative approaches for justifying the adaptiveness of individual RNA editing sites are still lacking. We performed a comparative genomic analysis on 113 Diptera species, focusing on the Adar Ser>Gly auto-recoding site in Drosophila . We only found one species having a derived Gly at the corresponding site, and this occurrence was significantly lower than genome-wide random expectation. This suggests that the Adar Ser>Gly site is unlikely to be genomically replaced with G during evolution, and thus indicating the advantage of editable status over hardwired genomic alleles. Similar trends were observed for the conserved Ile>Met recoding in gene Syt1 . In the light of evolution, we established a comparative genomic approach for quantitatively justifying the adaptiveness of individual editing sites. Priority should be given to such adaptive editing sites in future functional studies.

Conserved A-to-I RNA editing with non-conserved recoding expands the candidates of functional editing sites

“…This conformational change might affect the dynamics of the potassium channel where larger diameter enables higher ion permeability. More amazingly, similar to our previous finding in C. chinensis that this recoding level elevated under cold stress [ 24 ], in Drosophila the editing level at this site was also anti-correlated with temperature [ 43 ]. Thus, the recoded Shab protein with putatively higher ion permeability represents the cold-specific isoform ( Figure 5b ).…”