Enolase (2-phospho-D-glycerate hydrolase) is an enzymatic component of the glycolytic pathway and is conserved through evolution. The TR-CaENO1/Caeno1 stain, of which the expression of CaENO1 is under control of the tetracycline-regulatable (TR) expression system, is utilized for elucidating the functions of CaENO1 in Candida albicans. As expected, there was no detectable CaENO1 mRNA when the TR-CaENO1/Caeno1 cells grew on media containing doxycycline repressing the expression of TR-CaENO1.The TR-CaENO1/Caeno1 cells were arrested in media containing doxycycline in the presence of glucose but not in non-fermentable carbon sources, such as glycerol. Furthermore, the TR-CaENO1/Caeno1 cells were also arrested in media containing 4% serum. In this study, we have showed that CaENO1 is required for the cell growth of C. albicans in the presence of glucose. Our findings may help us to design new and more effective antifungal agents for preventing and treating bloodstream fungal infections by blocking the function(s) of enolases.
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| rdfs:comment |
Enolase (2-phospho-D-glycerate hydrolase) is an enzymatic component of the glycolytic pathway and is conserved through evolution. The TR-CaENO1/Caeno1 stain, of which the expression of CaENO1 is under control of the tetracycline-regulatable (TR) expression system, is utilized for elucidating the functions of CaENO1 in Candida albicans. As expected, there was no detectable CaENO1 mRNA when the TR-CaENO1/Caeno1 cells grew on media containing doxycycline repressing the expression of TR-CaENO1.The TR-CaENO1/Caeno1 cells were arrested in media containing doxycycline in the presence of glucose but not in non-fermentable carbon sources, such as glycerol. Furthermore, the TR-CaENO1/Caeno1 cells were also arrested in media containing 4% serum. In this study, we have showed that CaENO1 is required for the cell growth of C. albicans in the presence of glucose. Our findings may help us to design new and more effective antifungal agents for preventing and treating bloodstream fungal infections by blocking the function(s) of enolases.
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| skos:exactMatch | |
| uniprot:name |
J. Biomed. Sci.
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| uniprot:author |
Chen H.F.,
Kuo T.J.,
Lin C.Y.,
Yang Y.L.
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| uniprot:date |
2006
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| uniprot:pages |
313-321
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| uniprot:title |
Mutations on CaENO1 in Candida albicans inhibit cell growth in the presence of glucose.
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| uniprot:volume |
13
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| dc-term:identifier |
doi:10.1007/s11373-005-9054-6
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