This article discusses a recently published paper. In short, the authors of the paper found that:

"Our phylogenetic analysis of RPS23, a key protein in the ribosomal decoding center, uncovered a lysine residue almost universally conserved across all domains of life, which is replaced by an arginine in a small number of hyperthermophilic archaea. When introduced into eukaryotic RPS23 homologs, this mutation leads to accurate translation, as well as heat shock resistance and longer life, in yeast, worms, and flies."

"...we have consistently found a lysine residue to be remarkably conserved in the KQPNSA region of ribosomal RPS23, nearly invariant throughout evolution. The only exceptions to this rule are in the thermophilic and hyperthermophilic archea, where the amino acid lysine is replaced by arginine..."

It seems particularly exciting that a single amino acid change (induced in their experiments using CRISPR) can lead to a significant increase in thermo tolerance. The gene, RPS23, is also found in Arabidopsis at two locations (AT5G02960 and AT3G09680). I confirmed the sequence similarity by taking the coding sequence of the Drosophila RPS23 gene from IGB and Blasting it against the Arabidopsis genome. Examining the two Arabidopsis genes in IGB, both contain the KQPNSA region that is heavily conserved (as reported by the paper in figure 1C).

It would be very interesting to induce the same amino acid change (K -> R) in Arabidopsis and observe the effects on thermo tolerance.

This Jira ticket can serve as an example of how IGB can be used to quickly investigate genes and their sequence and translation in multiple organisms.