基因组学与应用生物学
基因組學與應用生物學
기인조학여응용생물학
GENOMICS AND APPLIED BIOLOGY
2013年
1期
91-96
,共6页
范晓军%宋志芳%仙笑笑%李瑶%赵秋勇*
範曉軍%宋誌芳%仙笑笑%李瑤%趙鞦勇*
범효군%송지방%선소소%리요%조추용*
金纹细蛾%几丁质酶%生物信息学分析%理化性质%系统发育树
金紋細蛾%幾丁質酶%生物信息學分析%理化性質%繫統髮育樹
금문세아%궤정질매%생물신식학분석%이화성질%계통발육수
Lithocolletis ringoniella%Chitinase%Bioinformatical analysis%Physical and chemical properties%Phylogenetic tree
本文从生物信息学角度对克隆获得的金纹细蛾几丁质酶进行分析,通过课题组提交到GenBank的数据,采用在线分析及相应软件分析预测金纹细蛾几丁质酶(LrCHI)基因核苷酸和氨基酸序列的组成、理化性质、信号肽、糖基化位点、磷酸化位点、疏水性、二级结构和三级结构等,并构建系统发育树.结果表明:LrCHI开放阅读框由1737 bp组成,推导578个氨基酸;此序列所编码的蛋白属于几丁质酶18家族,其N端含有信号肽和几丁质酶18家族活性位点,C端为几丁质结合区,无跨膜结构域区域;预测LrCHI为亲水性蛋白;金纹细蛾与鳞翅目的棉铃虫、甜菜夜蛾进化关系最近.分析结果可为LrCHI的科学研究提供有价值的信息,为进一步研究其高级结构与功能的关系提供理论依据.
本文從生物信息學角度對剋隆穫得的金紋細蛾幾丁質酶進行分析,通過課題組提交到GenBank的數據,採用在線分析及相應軟件分析預測金紋細蛾幾丁質酶(LrCHI)基因覈苷痠和氨基痠序列的組成、理化性質、信號肽、糖基化位點、燐痠化位點、疏水性、二級結構和三級結構等,併構建繫統髮育樹.結果錶明:LrCHI開放閱讀框由1737 bp組成,推導578箇氨基痠;此序列所編碼的蛋白屬于幾丁質酶18傢族,其N耑含有信號肽和幾丁質酶18傢族活性位點,C耑為幾丁質結閤區,無跨膜結構域區域;預測LrCHI為親水性蛋白;金紋細蛾與鱗翅目的棉鈴蟲、甜菜夜蛾進化關繫最近.分析結果可為LrCHI的科學研究提供有價值的信息,為進一步研究其高級結構與功能的關繫提供理論依據.
본문종생물신식학각도대극륭획득적금문세아궤정질매진행분석,통과과제조제교도GenBank적수거,채용재선분석급상응연건분석예측금문세아궤정질매(LrCHI)기인핵감산화안기산서렬적조성、이화성질、신호태、당기화위점、린산화위점、소수성、이급결구화삼급결구등,병구건계통발육수.결과표명:LrCHI개방열독광유1737 bp조성,추도578개안기산;차서렬소편마적단백속우궤정질매18가족,기N단함유신호태화궤정질매18가족활성위점,C단위궤정질결합구,무과막결구역구역;예측LrCHI위친수성단백;금문세아여린시목적면령충、첨채야아진화관계최근.분석결과가위LrCHI적과학연구제공유개치적신식,위진일보연구기고급결구여공능적관계제공이론의거.
In this paper we analyzed Lithocolletis ringoniella chitinase from the perspective of bioinformatics. Based on the data that had been submitted to GenBank by our group, Nucleotide sequence and deduced amino acid sequence of Lithocolletis ringoniella chitinase were analyzed and predicted by the tools of bioinformatics which are available online or corresponding software in the following aspects:the composition, physical and chemical prop-erties, signalpeptide, O-glycosylation site, phosphorylation site, hydrophobic character, secondary structure, ter-tiary structure, etc. We also built phylogenetic trees. The results showed that the open reading frame (ORF) ofLrCHI consists of 1 737 bp which deduces 578 amino acid sequences. The protein encoded by this sequence belongs to chitinase family 18. There are a signal peptide and a chitinase family 18 active site in the N-terminal region of the polypeptide chain. There is a chitin-binding site in the C-terminal region. No possible transmembrane domain re-gion. LrCHI might be a hydrophilic protein. Lithocolletis ringoniella, phylogenetic relationship is the nearest to Helicoverpa armigera and Spodoptera exigua than other insects. The result of this study may provided very valu-able information for experimental research and application development and theoretical basis for further study of the relationships between high-level structure and function.