Solubilization of Neurospora crassa Rodlet Proteins and Identification of the Predominant Protein as the Proteolytically Processed eas (ccg-2) Gene Product

Experimental Mycology Pub Date : 1995-06-01 DOI:10.1006/emyc.1995.1020

Matthew D. Templeton, David R. Greenwood, Ross E. Beever

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引用次数: 32

Abstract

Templeton, M. D., Greenwood, D. R., and Beever, R. E. 1995. Solubilization of Neurospora crassa rodlet proteins and identification of the predominant protein as the proteolytically processed eas (ccg-2) gene product. Experimental Mycology 19, 166-169. Proteins from conidial rodlet preparations of Neurospora crassa were solubilized in trifluoroacetic acid. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of solubilized rodlets revealed a predominant protein of approximately 7 kDa. This protein was absent from preparations of N. crassa cultures carrying the eas mutation. The protein was purified by reverse-phase high-performance liquid chromatography and the N-terminal amino acid sequence of the purified protein was found to be identical to an internal portion of the deduced amino acid sequence of eas. Comparison of the sequences indicates a 29-amino-acid leader which is cleaved to generate the mature protein.

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粗神经孢子虫rolet蛋白的溶解及蛋白水解eas (ccg-2)基因产物优势蛋白的鉴定

邓普顿，医学博士，格林伍德，医学博士和比弗，r.e. 1995。粗神经孢子虫棒状蛋白的增溶及优势蛋白水解eas (ccg-2)基因产物的鉴定真菌学通报，19(2):444 - 444。用三氟乙酸溶解粗神经孢子菌分生孢子小棒制剂中的蛋白质。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示溶解小颗粒的优势蛋白约为7 kDa。该蛋白在携带eas突变的草氮草培养物中不存在。用反相高效液相色谱法纯化该蛋白，发现其n端氨基酸序列与推导出的eas氨基酸序列的内部部分相同。序列比较表明，一个由29个氨基酸组成的先导体被裂解生成成熟蛋白。

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Experimental Mycology

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