![]() We describe a unique ribosomal DNA insertion, which is processed after rRNA transcription and breaks the NMR 28S rRNA into two distinct fragments. The connection between translation and aging led us to examine NMR ribosomes for longevity-promoting phenotypes such as altered translation rate and translational fidelity. In summary, our results show that naked mole-rat cells produce fewer aberrant proteins, supporting the hypothesis that the more stable proteome of the naked mole-rat contributes to its longevity. Although we cannot directly test whether the unique 28S rRNA structure contributes to the increased fidelity of translation, we speculate that it may change the folding or dynamics of the large ribosomal subunit, altering the rate of GTP hydrolysis and/or interaction of the large subunit with tRNA during accommodation, thus affecting the fidelity of protein synthesis. We report that naked mole-rat fibroblasts have significantly increased translational fidelity despite having comparable translation rates with mouse fibroblasts. Because this hidden break site could alter ribosome structure, we investigated whether translation rate and amino acid incorporation fidelity were altered. The excised fragment is unique to the naked mole-rat rRNA and does not show homology to other genomic regions. The two breakpoints are located in the 28S rRNA divergent region 6 and excise a fragment of 263 nt. Here we report that 28S ribosomal RNA (rRNA) of the naked mole-rat is processed into two smaller fragments of unequal size. ![]() ![]() Multiple data implicate modulation of protein translation in longevity. The naked mole-rat ( Heterocephalus glaber) is a subterranean eusocial rodent with a markedly long lifespan and resistance to tumorigenesis. ![]()
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