Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4371237 | Experimental Parasitology | 2010 | 9 Pages |
Abstract
Gene regulation in trypanosomatids occurs mainly by post-transcriptional mechanisms modulating mRNA stability and translation. We have investigated heat shock protein (HSP) 70 gene regulation in Trypanosoma cruzi, the causal agent of Chagas' disease. The HSP70 mRNA's half-life increases after heat shock, and the stabilization is dependent on protein synthesis. In a cell-free RNA decay assay, a U-rich region in the 3â² untranslated region (UTR) is a target for degradation, which is reduced when in the presence of protein extracts from heat shocked cells. In a transfected reporter gene assay, both the 5â²- and 3â²-UTRs confer temperature-dependent regulation. Both UTRs must be present to increase mRNA stability at 37 °C, indicating that the 5â²- and 3â²-UTRs act cooperatively to stabilize HSP70 mRNA during heat shock. We conclude that HSP70 5â²- and 3â²-UTRs regulate mRNA stability during heat shock in T. cruzi.
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Authors
Deivid C Rodrigues, Rosane Silva, Edson Rondinelli, Turán P Ãrményi,