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Reacting to Stress

When cells are subjected to stress, they shut down the export of the majority of mRNAs from the nucleus but still permit the export of mRNAs that encode for heat shock proteins that allow cells to deal with the stress. How the cell accomplishes this selective and specific mRNA export from the nucleus is to a large extent unknown.

In this Paper of the Week, Hollie S. Skaggs and colleagues have investigated the unexpected interaction between the transcription factor HSF1, which controls heat shock protein (HSP) gene expression after stress by binding to their promoters to induce expression, and the nucleopore-associating protein TPR under stress-inducing conditions. They show that in response to stress TPR interacts with HSF1, is recruited to the HSP70 promoter region, and preferentially associates with mRNA transcribed from the HSP70 promoter rather than from a non-stress-induced promoter. HSF1-TPR interaction is also required for the efficient export of heat shock protein mRNA from the nucleus after subjecting cells to stress. These findings elegantly show a direct functional connection between the first and a later stage in gene expression, i.e. transcription and mRNA export, during the cell's response to stress.

FOOTNOTES

See referenced article, J. Biol. Chem. 2007, 282, 33902-33907

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