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The Hsp70 member, Ssa1, acts as a DNA‐binding transcriptional co‐activator of laccase in Cryptococcus neoformans
Author(s) -
Zhang Shirong,
Hacham Moshe,
Panepinto John,
Hu Guowu,
Shin Soowan,
Zhu Xudong,
Williamson Peter R.
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05422.x
Subject(s) - cryptococcus neoformans , biology , virulence , hsp70 , activator (genetics) , laccase , transcription factor , virulence factor , heat shock protein , microbiology and biotechnology , transcription (linguistics) , gene , biochemistry , enzyme , linguistics , philosophy
Summary Hsp70 proteins are a well‐known class of chaperones that have also been described to have roles in cellular regulation. Here, we show that a Cryptococcus neoformans Hsp70 homologue Ssa1 acts as a DNA‐binding transcriptional co‐activator of the fungal virulence factor, laccase, via binding to a GC‐rich element within the 5′‐UAS in response to glucose starvation, iron, copper, calcium and temperature. In addition, Ssa1 forms a regulatory complex with heat shock transcription factor and TATA‐binding protein during laccase induction. Furthermore, deletion of Ssa1 results in reduced laccase and attenuated virulence using a mouse model. These results indicate that Hsp70 functions as a stress‐related transcriptional co‐activator required for fungal virulence.