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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Distinct translation regulation by two alternative 5'UTRs of a stress-responsive protein--dPrx I.

Translation efficiency is often regulated in part by 5'-untranslated region (5'UTR). Sequence analysis of an evolutionarily conserved stress-responsive protein, Drosophila Peroxiredoxin I (dPrx I), found the transcript to have two alternative 5'UTRs that lead to an identical coding sequence: namely Ia and Ib. Although both isoforms coexisted in Drosophila cells, the Ia isoform appeared to be dominant. Furthermore, reporter assay found that Ia enhanced translation in steady-state cells while Ib increased translation in cells under oxidative stress. Together, our data suggest that the two alternative 5'UTRs of dPrx I may be involved in a translational regulatory mechanism that responds to cellular oxidative stress.[1]

References

  1. Distinct translation regulation by two alternative 5'UTRs of a stress-responsive protein--dPrx I. Chen, C.W., Lin, T.Y., Chen, T.C., Juang, J.L. J. Biomed. Sci. (2005) [Pubmed]
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