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禾谷炭疽菌内吞相关蛋白找寻及其生物信息学
引用本文:覃悦,韩长志. 禾谷炭疽菌内吞相关蛋白找寻及其生物信息学[J]. 科学技术与工程, 2021, 21(13): 5287-5295. DOI: 10.3969/j.issn.1671-1815.2021.13.016
作者姓名:覃悦  韩长志
作者单位:西南林业大学生物多样性保护学院,昆明650224;西南林业大学研究生院,昆明650224;西南林业大学生物多样性保护学院,昆明650224;云南省森林灾害预警与控制重点实验室,昆明650224
基金项目:国家自然科学基金项目(面上项目,重点项目,重大项目)
摘    要:真菌通过内吞的质膜变形运动将细胞以外的物质转运到细胞内,有关植物病原丝状真菌中内吞作用相关蛋白及其特征研究尚不多见,对其发挥内吞作用的NPFxD相关蛋白尚未见报道.运用内吞作用关键词在NCBI数据库中搜索,同时,以模式生物构巢曲霉中NPFxD蛋白序列为基础,通过Blastp开展在线比对分析,明确禾谷炭疽菌中具有NPFxD基序的蛋白有6个,根据同源关系分别命名为CgTPO1、CgMYO2、CgCRN3、CgNPF4、CgGBP5和CgTRM6;并从跨膜、保守结构域、亚细胞定位、理化性质以及信号肽、二级结构等方面对上述蛋白开展生物信息学分析.结果表明,不同跨膜预测软件结果并不相同,保守结构域种类较多且缺少同一类结构域,蛋白亚细胞定位位置多样且不尽相同,尤以G、A氨基酸残基所占比例最高,仅CgNPF4具有明显的信号肽,而CgMYO2蛋白具有比例相对高的α螺旋结构.此外,通过遗传关系分析明确了禾谷炭疽菌中NPFxD蛋白和炭疽菌属病菌具有较高的同源性和较近的亲缘关系,为深入探索NPFxD基序蛋白在炭疽病中的功能奠定了坚实的理论基础.

关 键 词:内吞作用  禾谷炭疽菌  NPFxD基序  炭疽菌属  生物信息学
收稿时间:2020-08-03
修稿时间:2021-02-23

Bioinformatics of NPFxD motif Mediated Endocytosis-associated Proteins in Colletotrichum graminicola
Qin Yue,Han Changzhi. Bioinformatics of NPFxD motif Mediated Endocytosis-associated Proteins in Colletotrichum graminicola[J]. Science Technology and Engineering, 2021, 21(13): 5287-5295. DOI: 10.3969/j.issn.1671-1815.2021.13.016
Authors:Qin Yue  Han Changzhi
Affiliation:The Key Laboratory of Forest Disaster Warning and Control of Yunnan Province
Abstract:Substances outside the cell are transported into the cell through the deformation movement of the plasma membrane endocytosed by the fungus. Studies on endocytosis-related proteins and their characteristics in plant pathogenic filamentous fungi are still rare. The NPFxD-related proteins that exert endocytosis in plant pathogenic filamentous fungi have not been reported yet. Based on previous studies, and endocytosis keywords were used for searching in the NCBI database. At the same time, based on the sequence of the NPFxD motif protein in the model organism Aspergillus nidulans, online comparison analysis was carried out through Blastp. It is clear that there are 6 proteins with NPFxD motif in Colletotrichum graminicola, which are named CgTPO1, CgMYO2, CgCRN3, CgNPF4, CgGBP5 and CgTRM6 according to the homology relationship. In addition, the NPFxD protein has been analyzed in bioinformatics in terms of transmembrane, conserved domains, subcellular localization, physical and chemical properties, signal peptide, and secondary structure. The results show that the results of different transmembrane prediction software are not the same. There are many types of NPFxD protein conserved domains and lack of the same type of domains. The subcellular location of NPFxD protein is diverse and not the same. Gly and Ala amino acid residues account for the highest proportion and only CgNPF4 has an obvious signal peptide in NPFxD protein. Also, The CgMYO2 protein has a relatively high proportion of alpha helix structure. In addition, the genetic relationship analysis showed that the NPFxD protein of C. graminicola and the bacteria of the genus Colletotrichum had high homology and close genetic relationship. This research lays a solid theoretical foundation for further research on the function of NPFxD motif protein. At the same time, it also provides important theoretical guidance for further research on other Colletotrichum sp..
Keywords:Endocytosis   Colletotrichum graminicola   NPFxD motif   Colletotrichum   Bioinformatics
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