Isolation and identification of a 92-kDa stress induced protein from Candida albicans

Isolation and identification of a 92-kDa stress induced protein from Candida albicans
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DOI:
10.1023/a:1007036518330
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发表时间:
1999-07-01
期刊:
影响因子:
5.5
通讯作者:
Larsen, B
Larsen, B
中科院分区:
生物学3区
文献类型:
--
作者:
Burt, ET;O'Connor, C;Larsen, B

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相似文献

先前的研究表明,雌激素的存在可以增强白色念珠菌在热和氧化应激下的存活率。白色念珠菌中的热休克和雌激素可诱导 92 kDa 蛋白质。先前的研究将这种蛋白质描述为 hsp90,因为它的分子大小和热诱导性(如电泳凝胶和蛋白质印迹中所见)。在本研究中,使用离子交换、羟基磷灰石和尺寸排阻色谱来分离 92 kDa 蛋白质条带。印迹到PVDF膜上的分离蛋白的N端序列确定为V-Q-S-α-V-L-G-F-P-R。该序列与来自酿酒酵母的 MET6 基因产物(不依赖于钴胺素的甲硫氨酸合酶)的 N 端序列同源。这项研究的结果表明,白色念珠菌中的不依赖于钴胺素的甲硫氨酸合酶同系物可以被热和雌激素诱导。这项研究还表明,念珠菌 hsp90 更有可能以 82 kDa 蛋白质的形式存在,如先前描述的 cDNA 预测的那样,而不是如文献报道的以 92 kDa 蛋白质的形式存在。
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.