Post-transcriptional regulation of the trypanosome heat shock response by a zinc finger protein

In most organisms, the heat-shock response involves increased heat-shock gene transcription. In Kinetoplastid protists, however, virtually all control of gene expression is post-transcriptional. Correspondingly, Trypanosoma brucei heat-shock protein 70 (HSP70) synthesis after heat shock depends on r...

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Veröffentlicht in:PLoS pathogens 2013-04, Vol.9 (4), p.e1003286-e1003286
Hauptverfasser: Droll, Dorothea, Minia, Igor, Fadda, Abeer, Singh, Aditi, Stewart, Mhairi, Queiroz, Rafael, Clayton, Christine
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container_title PLoS pathogens
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creator Droll, Dorothea
Minia, Igor
Fadda, Abeer
Singh, Aditi
Stewart, Mhairi
Queiroz, Rafael
Clayton, Christine
description In most organisms, the heat-shock response involves increased heat-shock gene transcription. In Kinetoplastid protists, however, virtually all control of gene expression is post-transcriptional. Correspondingly, Trypanosoma brucei heat-shock protein 70 (HSP70) synthesis after heat shock depends on regulation of HSP70 mRNA turnover. We here show that the T. brucei CCCH zinc finger protein ZC3H11 is a post-transcriptional regulator of trypanosome chaperone mRNAs. ZC3H11 is essential in bloodstream-form trypanosomes and for recovery of insect-form trypanosomes from heat shock. ZC3H11 binds to mRNAs encoding heat-shock protein homologues, with clear specificity for the subset of trypanosome chaperones that is required for protein refolding. In procyclic forms, ZC3H11 was required for stabilisation of target chaperone-encoding mRNAs after heat shock, and the HSP70 mRNA was also decreased upon ZC3H11 depletion in bloodstream forms. Many mRNAs bound to ZC3H11 have a consensus AUU repeat motif in the 3'-untranslated region. ZC3H11 bound preferentially to AUU repeats in vitro, and ZC3H11 regulation of HSP70 mRNA in bloodstream forms depended on its AUU repeat region. Tethering of ZC3H11 to a reporter mRNA increased reporter expression, showing that it is capable of actively stabilizing an mRNA. These results show that expression of trypanosome heat-shock genes is controlled by a specific RNA-protein interaction. They also show that heat-shock-induced chaperone expression in procyclic trypanosome enhances parasite survival at elevated temperatures.
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subjects Bacterial proteins
Biology
Cell Line
Experiments
Gene expression
Gene Expression Regulation
Genetic aspects
Genetic transcription
Heat
Heat shock proteins
Heat-Shock Response - genetics
HSP70 Heat-Shock Proteins - genetics
HSP70 Heat-Shock Proteins - metabolism
Humans
Mammals
Messenger RNA
Observations
Properties
Protein Binding
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
RNA Interference
RNA polymerase
RNA Processing, Post-Transcriptional
RNA Splicing
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA, Protozoan - genetics
RNA, Protozoan - metabolism
RNA, Small Interfering
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
RNA-protein interactions
Sequence Alignment
Temperature
Testing
Trypanosoma brucei
Trypanosoma brucei brucei - genetics
Trypanosoma brucei brucei - metabolism
Zinc finger proteins
Zinc Fingers - genetics
title Post-transcriptional regulation of the trypanosome heat shock response by a zinc finger protein
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