The Hsp70 member, Ssa1, acts as a DNA‐binding transcriptional co‐activator of laccase in  Cryptococcus neoformans | Zendy

Zhang Shirong | Zendy; Hacham Moshe | Zendy; Panepinto John | Zendy; Hu Guowu | Zendy; Shin Soowan | Zendy; Zhu Xudong | Zendy; Williamson Peter R. | Zendy

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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.

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