Trypanosoma cruzi: Modulation of HSP70 mRNA stability by untranslated regions during heat shock
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 s...
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Published in | Experimental parasitology Vol. 126; no. 2; pp. 245 - 253 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier Inc
01.10.2010
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | 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 3′ 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 5′- and 3′-UTRs confer temperature-dependent regulation. Both UTRs must be present to increase mRNA stability at 37
°C, indicating that the 5′- and 3′-UTRs act cooperatively to stabilize
HSP70 mRNA during heat shock. We conclude that
HSP70 5′- and 3′-UTRs regulate mRNA stability during heat shock in
T. cruzi. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-4894 1090-2449 |
DOI: | 10.1016/j.exppara.2010.05.009 |