Aminoacyl-tRNA synthetase gene alignments from multiple Sileneae species generated from full-length transcripts using Iso-Seq and raw microscopy image files

Trimmed and untrimmed alignments for the final aminoacyl-tRNA synthetases
in Sileneae species and Arabidopsis thaliana.
We investigated the evolution of subcellular localization of aaRS enzymes
in five different species from the plant
lineage Sileneae that has experienced extensive and
rapid mitochondrial tRNA loss. By analyzing full-length mRNA transcripts
with single-molecule sequencing technology (PacBio Iso-Seq) and searching
genome sequences, we found instances of predicted retargeting of an
ancestrally cytosolic aaRS to the mitochondrion as well as scenarios where
enzyme localization does not appear to change despite functional tRNA
replacement. Nikon .nd2 raw microscopy files for the transient expression
and imaging of predicted transit peptides and colocalization assays in N.
benthamiana epithelial cells. The amino acid sequence
plus 10 upstream amino acids of the protein body were fused to GFP and
co-transfected with an eqFP611-tagged transit peptide from a known
mitochondrially localized protein (isovaleryl-CoA dehydrogenase).