New computational methods reveal tRNA identity element divergence between Proteobacteria and Cyanobacteria.
There are at least 21 subfunctional classes of tRNAs in most cells that, despite a very highly conserved and compact common structure, must interact specifically with different cliques of proteins or cause grave organismal consequences. Protein recognition of specific tRNA substrates is achieved in part through class-restricted tRNA features called tRNA identity determinants. In earlier work we used TFAM, a statistical classifier of tRNA function, to show evidence of unexpectedly large diversity among bacteria in tRNA identity determinants. We also created a data reduction technique called function logos to visualize identity determinants for a given taxon. Here we show evidence that determinants for lysylated isoleucine tRNAs are not the same in Proteobacteria as in other bacterial groups including the Cyanobacteria. Consistent with this, the lysylating biosynthetic enzyme TilS lacks a C-terminal domain in Cyanobacteria that is present in Proteobacteria. We present here, using function logos, a map estimating all potential identity determinants generally operational in Cyanobacteria and Proteobacteria. To further isolate the differences in potential tRNA identity determinants between Proteobacteria and Cyanobacteria, we created two new data reduction visualizations to contrast sequence and function logos between two taxa. One, called Information Difference logos (ID logos), shows the evolutionary gain or retention of functional information associated to features in one lineage. The other, Kullback-Leibler divergence Difference logos (KLD logos), shows recruitments or shifts in the functional associations of features, especially those informative in both lineages. We used these new logos to specifically isolate and visualize the differences in potential tRNA identity determinants between Proteobacteria and Cyanobacteria. Our graphical results point to numerous differences in potential tRNA identity determinants between these groups. Although more differences in general are explained by shifts in functional association rather than gains or losses, the apparent identity differences in lysylated isoleucine tRNAs appear to have evolved through both mechanisms.
Freyhult
Eva
E
The Linnaeus Centre for Bioinformatics, Uppsala University, Box 598, 751 24 Uppsala, Sweden.
Cui
Yuanyuan
Y
Nilsson
Olle
O
Ardell
David H
DH
D000465:Algorithms; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D000458:Cyanobacteria / Q000235:genetics* / Q000378:metabolism; D020560:Proteobacteria / Q000235:genetics* / Q000378:metabolism; D012343:RNA, Transfer / Q000235:genetics*; D012346:RNA, Transfer, Amino Acyl / Q000235:genetics
D012346:RNA, Transfer, Amino Acyl; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases