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Molecular and Cellular Biology, February 2007, p. 1505-1515, Vol. 27, No. 4
0270-7306/07/$08.00+0 doi:10.1128/MCB.01158-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 813A Stellar-Chance, 422 Curie Blvd., Philadelphia, Pennsylvania 19104-6059
Received 27 June 2006/ Returned for modification 12 September 2006/ Accepted 17 November 2006
In Saccharomyces cerevisiae, the intracellular concentration of trehalose increases rapidly in response to many environmental stresses, including heat shock. These high trehalose levels have been correlated with tolerance to adverse conditions and led to the model that trehalose functions as a chemical cochaperone. Here, we show that the transcriptional activity of Hsf1 during the heat shock response depends on trehalose. Strains with low levels of trehalose have a diminished transcriptional response to heat shock, while strains with high levels of trehalose have an enhanced transcriptional response to heat shock. The enhanced transcriptional response does not require the other heat-responsive transcription factors Msn2/4 but is dependent upon heat and Hsf1. In addition, the phosphorylation levels of Hsf1 correlate with both transcriptional activity and the presence of trehalose. These in vivo results support a new role for trehalose, where trehalose directly modifies the dynamic range of Hsf1 activity and therefore influences heat shock protein mRNA levels in response to stress.
Published ahead of print on 4 December 2006.
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