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J Med Microbiol 55 (2006), 1403-1411; DOI: 10.1099/jmm.0.46650-0
© 2006 Society for General Microbiology
ISSN 1473-5644

The DNA-binding domain of CaNdt80p is required to activate CDR1 involved in drug resistance in Candida albicans

Jang-Shiun Wang1,2, Yun-Liang Yang3, Chin-Jung Wu3, Karen J. Ouyang3, Kuo-Yun Tseng2, Chia-Geun Chen2, Hsin Wang3 and Hsiu-Jung Lo2

1 Graduate Institute of Life Sciences, National Defence Medical Center, Taipei, Taiwan, Republic of China

2 Division of Clinical Research, National Health Research Institutes, 35 Keyan Road, Zhunan Town, Miaoli County 350, Taiwan, Republic of China

3 Department of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan, Republic of China

Correspondence
Hsiu-Jung Lo
hjlo{at}nhri.org.tw

Received 28 March 2006
Accepted 13 July 2006

CaNdt80p, the Candida albicans homologue of the Saccharomyces cerevisiae transcription factor ScNdt80p, has been identified as a positive regulator of CDR1, which encodes an efflux pump involved in drug resistance in C. albicans. To investigate the involvement of the putative DNA-binding domain of CaNdt80p in drug resistance, chimeras of CaNdt80p and ScNdt80p were constructed. Interestingly, the DNA-binding domain of ScNdt80p could functionally complement that of CaNdt80p to activate CDR1p–lacZ in S. cerevisiae. Consistently, CaNdt80p containing a mutation in the DNA-binding domain failed to activate CDR1p–lacZ in S. cerevisiae. Furthermore, a copy of CaNDT80 with the same mutation also failed to complement the drug-sensitive phenotype caused by a null mutation in C. albicans. Thus, the DNA-binding domain of CaNdt80p is critical for its function in drug resistance in C. albicans.

Abbreviations: ß-Gal, ß-galactosidase.




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