HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA.
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.[1]References
- HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA. Skaggs, H.S., Xing, H., Wilkerson, D.C., Murphy, L.A., Hong, Y., Mayhew, C.N., Sarge, K.D. J. Biol. Chem. (2007) [Pubmed]
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