Despite the potential for many possible secondary-structure conformations, the native sequence of ribosomal RNA (rRNA) is able to find the correct and universally conserved core fold. This study reports a computational analysis investigating two mechanisms that appear to constrain rRNA secondary-structure conformational space: ribosomal proteins and rRNA sequence composition. The analysis was carried out by using rRNA-ribosomal protein interaction data for the Escherichia coli 16S rRNA and free energy minimization software for secondary-structure prediction. The results indicate that selection pressures on rRNA sequence composition and ribosomal protein-rRNA interaction play a key role in constraining the rRNA secondary structure to a single stable form.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1214544 | PMC |
| http://dx.doi.org/10.1093/nar/gki805 | DOI Listing |
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