Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 282, Issue 47, Pages 33902-33907Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M704054200
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Funding
- NICHD NIH HHS [HD 50043, F32 HD050043] Funding Source: Medline
- NIEHS NIH HHS [T32 ES 007266] Funding Source: Medline
- NIGMS NIH HHS [R01 GM064606-03, GM 61053, GM 64606, R01 GM061053-01A1, R01 GM064606, R01 GM061053, R01 GM064606-04, R01 GM061053-04, R01 GM064606-01A2, R01 GM061053-03, R01 GM061053-02, R01 GM064606-02] Funding Source: Medline
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Stress conditions inhibit mRNA export, but mRNAs encoding heat shock proteins continue to be efficiently exported from the nucleus during stress. How HSP mRNAs bypass this stress-associated export inhibition was not known. Here, we show that HSF1, the transcription factor that binds HSP promoters after stress to induce their transcription, interacts with the nuclear pore-associating TPR protein in a stress-responsive manner. TPR is brought into proximity of the HSP70 promoter after stress and preferentially associates with mRNAs transcribed from this promoter. Disruption of the HSF1-TPR interaction inhibits the export of mRNAs expressed from the HSP70 promoter, both endogenous HSP70 mRNA and a luciferase reporter mRNA. These results suggest that HSP mRNA export escapes stress inhibition via HSF1-mediated recruitment of the nuclear pore-associating protein TPR to HSP genes, thereby functionally connecting the first and last nuclear steps of the gene expression pathway, transcription and mRNA export.
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