Article ID Journal Published Year Pages File Type
2048753 FEBS Letters 2010 9 Pages PDF
Abstract

I review recent developments in computational analysis of tRNA identity. I suggest that the tRNA–protein interaction network is hierarchically organized, and coevolutionarily flexible. Its functional specificity of recognition and discrimination persists despite generic structural constraints and perturbative evolutionary forces. This flexibility comes from its arbitrary nature as a self-recognizing shape code. A revisualization of predicted Proteobacterial tRNA identity highlights open research problems. tRNA identity elements and their coevolution with proteins must be mapped structurally over the Tree of Life. These traits can also resolve deep roots in the Tree. I show that histidylation identity elements phylogenetically reposition Pelagibacter ubique within alpha-Proteobacteria.

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