Characterization of an Extracellular Serine Protease Gene from the Nematophagous Fungus Lecanicillium psalliotae
Characterization of an Extracellular Serine Protease Gene from the Nematophagous Fungus Lecanicillium psalliotae
复制标题
DOI：
10.1007/s10529-005-0482-1
复制
发表时间：
2005-09
影响因子：
2.7
通讯作者：
Jinkui Yang;Xiaowei Huang;B. Tian;Hui Sun;J. Duan;Wenping Wu;Keqin Zhang
中科院分区：
文献类型：
--
作者：
Jinkui Yang;Xiaowei Huang;B. Tian;Hui Sun;J. Duan;Wenping Wu;Keqin Zhang
采用3′和5′ RACE（rapid amplification of cDNA ends）方法，从3个蜡蚧菌（Lecanicillium psalliotae）分离物中克隆到编码表皮降解丝氨酸蛋白酶的基因。该基因编码382个氨基酸，该蛋白与枯草杆菌蛋白酶N和肽酶S8共享保守基序。比较三个分离株的翻译cDNA序列，发现在位置230的氨基酸多态性。推导的蛋白酶序列与其他食草真菌表皮降解蛋白酶具有高度的相似性。
The gene encoding a cuticle-degrading serine protease was cloned from three isolates ofLecanicillium psalliotae(syn.Verticillium psalliotae) by 3′ and 5′ RACE (rapid amplification of cDNA ends) method. The gene encodes for 382 amino acids and the protein shares conserved motifs with subtilisin N and peptidase S8. Comparison of translated cDNA sequences of three isolates revealed one amino acid polymorphism at position 230. The deduced protease sequence shared high degree of similarities to other cuticle-degrading proteases from other nematophagous fungi.