Fig. 3: Microsporidian rRNA trades favorable folding for minimal length. | Nature Communications

Fig. 3: Microsporidian rRNA trades favorable folding for minimal length.

From: Adaptation to genome decay in the structure of the smallest eukaryotic ribosome

Fig. 3

Structure of the helix H18 of the 25 S rRNA in S. cerevisiae, V. necatrix, and E. cuniculi. Typically, in ribosomes across the three domains of life, this linker is folded into an RNA helix, which comprises between 24 and 34 residues. By contrast, in microsporidia this rRNA linker is being progressively reduced to two, single-stranded uridine-rich linkers that comprise just 12 residues. Most of these residues are exposed to the solvent. This figure illustrates that microsporidian parasites appear to defy a common principle of rRNA folding, in which rRNA bases are typically paired with other bases or involved in rRNA–protein interactions. In microsporidia, some rRNA segments adopt unfavorable folding, in which former rRNA helices are turned into single-stranded segments that are stretched out almost into a straight line. Having these unusual stretches allows microsporidian rRNA to connect distant segments of rRNA using the minimal number of RNA bases.

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