HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA

Hollie S. Skaggs, Hongyan Xing, Donald C. Wilkerson, Lynea A. Murphy, Yiling Hong, Christopher N. Mayhew, Kevin D. Sarge

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


Stress conditions inhibit mRNA export, but mRNA sencoding 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.

Original languageEnglish
Pages (from-to)33902-33907
Number of pages6
JournalJournal of Biological Chemistry
Issue number47
StatePublished - Nov 23 2007

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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