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当前位置: 首页 > 文章 > 松材线虫Bx-ubc-3基因克隆及泛素通路鉴定 森林工程 2019 (5) 9-15
Position: Home > Articles > Genetic Cloning of Bx-ubc-3 and Identification of Ubiquitin Pathway from Bursaphelenchus xylophilus (Aphelenchida: Aphelenchoididae) Forest Engineering 2019 (5) 9-15

松材线虫Bx-ubc-3基因克隆及泛素通路鉴定

作  者：
许佳瑶;陈俏丽;张瑞芝;李丹蕾
单  位：
东北林业大学林学院
关键词：
松材线虫;泛素结合酶3;E2;泛素途径
摘  要：
泛素途径可以调节许多关键的细胞功能。为探究松材线虫中是否存在泛素途径以及泛素途径中的关键酶基因—泛素结合酶基因ubc3,构建松材线虫c DNA文库,并进行测序、ORF分析、同源性分析、系统发育树构建、蛋白相互作用预测和分子动力学模拟等工作。克隆到长度为957bp的Bx-ubc-3基因片段。随后的序列分析表明,其开放阅读框长度为738bp,编码245个氨基酸;氨基6酸同源性分析结果表明,Bx-UBC-3与已知的泛素结合酶高度同源;蛋白互作和分子对接分析及分子动力学模拟结果表明,Bx-UBC-3的结合位点位于一个α螺旋、一个Loop1(L1)环与一个Loop2(L2)环;形成硫酯的Cys103位于L2上,构成催化裂隙; Bx-UBC-3和Bx-Rbx1之间以及Bx-UBC-3和Bx-泛素之间形成氢键。这些结果表明松材线虫中存在一条理论泛素通路,其中的关键酶Bx-UBC-3是开发高效抗线虫生物药剂的潜在靶标。
译  名：
Genetic Cloning of Bx-ubc-3 and Identification of Ubiquitin Pathway from Bursaphelenchus xylophilus (Aphelenchida: Aphelenchoididae)
作  者：
XU Jiayao;CHEN Qiaoli;ZHANG Ruizhi;LI Danlei;College of Forestry,Northeast Forestry University;
单  位：
XU Jiayao%CHEN Qiaoli%ZHANG Ruizhi%LI Danlei%College of Forestry,Northeast Forestry University
关键词：
Bursaphelenchus xylophilus;;ubiquitin-conjugating enzyme 3;;E2;;ubiquitin pathway
摘  要：
The ubiquitin pathway is able to regulate many critical cellular functions. In order to explore the existence of the ubiquitin pathway and a key enzyme gene in ubiquitin pathway,ubiquitin-conjugating enzyme named as ubc3 in B. xylophilus,a c DNA library of B. xylophilus was constructed and sequenced,ORF analysis,homology analysis,phylogenetic tree construction,protein interaction prediction,docking and molecular dynamics simulation were carried out. The full-length c DNA generated by the nematode spliced leader method was 957 bp. Analysis of the Bx-ubc-3 c DNA sequence indicated that its open reading frame( ORF) was 783 bp and 245 amino acids were encoded. Comparison of the identified amino acid sequence with the current databases revealed extensive homology of Bx-ubc-3 to all known ubiquitin-conjugating enzymes. The modeling and prediction of protein interaction,docking and molecular dynamics simulations showed that the binding sites in Bx-ubc-3 were located in α helix,Loop 1( L1) ring and Loop 2( L2) ring. The thioester-forming Cys103,which was located in L2,constituted a catalytic cleft. The interfaces of Bx-ubc-3 to Bx-Rbx1 and Bx-ubc-3 to Bx-Ubiquitin were also supported by several obvious hydrogen bond interactions. Results show that there is a theoretic ubiquitin pathway in B. xylophilus,and support the notion that Bx-ubc-3 is a potential target for developing potent antinematodal drugs against B. xylophilus.

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