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Isolation and identification of a 92-kDa stress induced protein from Candida albicans.
- Source :
-
Mycopathologia [Mycopathologia] 1999; Vol. 147 (1), pp. 13-20. - Publication Year :
- 1999
-
Abstract
- It was previously shown that the presence of estrogen enhances survival of Candida albicans under heat and oxidative stresses. A 92-kDa protein is inducible by heat shock and estrogen in C. albicans. Previous studies have described this protein as hsp90 because of its molecular size and heat inducibility as seen on electrophoretic gels and Western blots. In this study, ion exchange, hydroxyapatite and size exclusion chromatography were used to isolate a 92-kDa-protein band. The N-terminal sequence of isolated protein blotted onto a PVDF membrane was determined to be V-Q-S-?-V-L-G-F-P-R. This sequence is homologous to the N-terminal sequence of the MET6 gene product, cobalamin-independent methionine synthase, from Saccharomyces cerevisiae. The results of this study suggest that a cobalamin-independent methionine synthase homolog is inducible by heat and estrogen in C. albicans. This study also suggests that Candida hsp90 is more likely to exist as an 82-kDa protein as predicted by a previously described cDNA and not as a 92-kDa protein as reported in the literature.
- Subjects :
- Amino Acid Sequence
Animals
Antibodies, Fungal chemistry
Blotting, Western
Candida albicans genetics
Chromatography, Ion Exchange
Durapatite chemistry
Electrophoresis, Polyacrylamide Gel
Estradiol physiology
Fungal Proteins chemistry
HSP90 Heat-Shock Proteins chemistry
Humans
Image Processing, Computer-Assisted
Luminescent Measurements
Molecular Sequence Data
Rats
Rats, Sprague-Dawley
Sequence Analysis, Protein
Candida albicans chemistry
Fungal Proteins isolation & purification
Gene Expression Regulation, Fungal
HSP90 Heat-Shock Proteins isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0301-486X
- Volume :
- 147
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Mycopathologia
- Publication Type :
- Academic Journal
- Accession number :
- 10872511
- Full Text :
- https://doi.org/10.1023/a:1007036518330