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.
Chen
Chien-Wen
CW
Division of Molecular and Genomic Medicine, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350, Taiwan.
Lin
Tzu-Yang
TY
Chen
Tsan-Chi
TC
Juang
Jyh-Lyh
JL
D020121:5' Untranslated Regions; D017398:Alternative Splicing; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers; D004330:Drosophila; D005091:Exons; D010544:Peroxidases / Q000235:genetics*; D054464:Peroxiredoxins; D014176:Protein Biosynthesis; D020133:Reverse Transcriptase Polymerase Chain Reaction
D020121:5' Untranslated Regions; D017931:DNA Primers; D010544:Peroxidases; D054464:Peroxiredoxins