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从昆虫病原真菌球孢白僵菌中克隆一种角质层降解蛋白酶

Cloning of a cuticle-degrading protease from the entomopathogenic fungus, Beauveria bassiana.

作者信息

Joshi L, St Leger R J, Bidochka M J

机构信息

Boyce Thompson Institute, Ithaca, NY 14853-1801.

出版信息

FEMS Microbiol Lett. 1995 Jan 15;125(2-3):211-7. doi: 10.1111/j.1574-6968.1995.tb07360.x.

Abstract

A Beauveria bassiana extracellular subtilisin-like serine endoprotease is a potential virulence factor by virtue of its activity against insect cuticles. A cDNA clone of the protease was isolated from mycelia of B. bassiana grown on cuticle/chitin cultures. The amino acid sequence of this gene was compared to that of Metarhizium anisopliae Pr1, the only pathogenicity determinant so far described from an entomopathogenic fungus, and proteinase K, isolated from Tritirachium album, a saprophytic fungus. The cDNA sequence revealed that B. bassiana Pr1 is synthesized as a large precursor (M(r) 37,460) containing a signal peptide, a propeptide and the mature protein predicted to have an M(r) of 26,832.

摘要

球孢白僵菌胞外类枯草杆菌丝氨酸内切蛋白酶因其对昆虫表皮的活性而成为一种潜在的致病因子。从在表皮/几丁质培养基上生长的球孢白僵菌菌丝体中分离出该蛋白酶的一个cDNA克隆。将该基因的氨基酸序列与金龟子绿僵菌Pr1(迄今为止从一种昆虫病原真菌中描述的唯一致病性决定因素)以及从腐生真菌特异腐质霉中分离出的蛋白酶K的氨基酸序列进行了比较。cDNA序列显示,球孢白僵菌Pr1以一种大的前体(分子量37,460)形式合成,该前体包含一个信号肽、一个前肽和预测分子量为26,832的成熟蛋白。

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