Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/ncomms11704
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Funding
- Sir Henry Wellcome Postdoctoral Fellowship (Wellcome Trust) [096072]
- Wellcome Trust-Massachusetts Institute of Technology (MIT) Postdoctoral Fellowship
- Canada Research Chair in Microbial Genomics and Infectious Disease
- Canadian Institutes of Health Research Grants [MOP-119520, MOP-86452]
- UK Biotechnology and Biological Sciences Research Council [BB/F00513X/1]
- European Research Council [ERC-2009-AdG-249793-STRIFE]
- Science and Technology Development Fund of Macau S.A.R (FDCT) [085/2014/A2]
- Research and Development Administrative Office of the University of Macau [SRG2014-00003-FHS]
- Burroughs Wellcome fund
- NIH [R15AO094406]
- Biotechnology and Biological Sciences Research Council [BB/F00513X/1, BB/M012360/1] Funding Source: researchfish
- BBSRC [BB/M012360/1, BB/F00513X/1] Funding Source: UKRI
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Fever is a universal response to infection, and opportunistic pathogens such as Candida albicans have evolved complex circuitry to sense and respond to heat. Here we harness RNA-seq and ChIP-seq to discover that the heat shock transcription factor, Hsf1, binds distinct motifs in nucleosome-depleted promoter regions to regulate heat shock genes and genes involved in virulence in C. albicans. Consequently, heat shock increases C. albicans host cell adhesion, damage and virulence. Hsf1 activation depends upon the molecular chaperone Hsp90 under basal and heat shock conditions, but the effects are opposite and in part controlled at the level of Hsf1 expression and DNA binding. Finally, we demonstrate that Hsp90 regulates global transcription programs by modulating nucleosome levels at promoters of stress-responsive genes. Thus, we describe a mechanism by which C. albicans responds to temperature via Hsf1 and Hsp90 to orchestrate gene expression and chromatin architecture, thereby enabling thermal adaptation and virulence.
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