摘要
FNR蛋白是蓝藻光能转换和能量代谢中的核心蛋白质,为了掌握该蛋白的生物信息学信息及其进化关系,选择具有研究和应用价值的7种模式蓝藻来源的FNR蛋白作为材料,以氨基酸序列为基础,采用ProtParam、Sompa、SWISS-MODEL及MEGA11等生物信息学工具对蓝藻FNR蛋白的结构、功能及进化关系进行分析。结果表明:蓝藻FNR蛋白均属于胞内表达的单亚基蛋白,无信号肽,无跨膜结构域。其氨基酸数目在370-440个之间,分子量在45 kD左右,理论等电点在5.5-6.0之间,不稳定性指数在40%左右,蛋白序列中存在保守的FAD及NADPH结合结构域及C末端的RWHVETY保守基序。蛋白的二级结构元件中,α-螺旋和β折叠比例在20%-30%之间,无规卷曲比例较高,普遍在47%左右。FNR蛋白的三级结构具有高度的结构相似性,蛋白质的N端普遍存在一段无序的无规卷曲结构,且暴露于蛋白质核心结构外侧。进化分析表明蓝藻FNR蛋白属于独立的进化分支,与高等植物来源的FNR蛋白的亲缘关系更近。本研究结果有助于深化对FNR蛋白的结构和功能的理解,同时也为FNR蛋白在藻类合成生物学的研究和应用提供参考。
FNR protein is a core protein in light energy conversion and energy metabolism of cyanobacteria.In order to grasp the bioinformatics information of this protein and its evolutionary relationship,seven FNR proteins from model cyanobacteria with research and application value were selected as materials and analyzed on the basis of amino acid sequences using bioinformatics tools,such as ProtParam,Sompa,SWISS-MODEL and MEGA11,to analyze the structure,function and evolutionary relationship of cyanobacterial FNR proteins.Bioinformatics tools such as ProtParam,Sompa,SWISS-MODEL and MEGA11 were used to analyze the structure,function and evolutionary relationship of cyanobacterial FNR proteins.The results showed that the cyanobacterial FNR proteins were all single-subunit proteins expressed intracellularly without signal peptide and transmembrane structural domains.The number of amino acids is between 370-440,the molecular weight is around 45 kD,the theoretical isoelectric point is between 5.5-6.0,the instability index is around 40%,and there are conserved FAD and NADPH-binding structural domains and conserved motifs of RWHVETY at the C-terminal end in the protein sequence.The proportion ofα-helix andβ-folding in the protein's secondary structural elements ranged from 20%to 30%,and the proportion of random curls was higher,generally around 47%.The tertiary structure of FNR proteins had a high degree of structural similarity,with a segment of disordered random curls prevailing at the N-terminal end of the proteins and being exposed to the outside of the core structure of the proteins.Evolutionary analyses indicated that cyanobacterial FNR proteins belong to an independent evolutionary branch and are more closely related to FNR proteins of higher plant origin.The results of this study help to deepen the understanding of the structure and function of FNR proteins,and also provide a reference for the research and application of FNR proteins in algal synthetic biology.
作者
殷亮
王代玮
韩雪雪
王丽娟
刘海燕
罗光宏
Yin Liang;Wang Dai-wei;Han Xue-xue;Wang Li-juan;Liu Hai-yan;Luo Guang-hong(Gansu Microalgae Engineering and Technology Research Center/Gansu Microalgae Technology Innovation Center,Hexi University;School of Agricultural and Ecological Engineering,Hexi University,Zhangye Gansu 734000)
出处
《河西学院学报》
2023年第5期45-53,共9页
Journal of Hexi University
基金
甘肃省高等学校创新基金项目(项目编号:2020A-105)
甘肃省重点研发计划-社发类(项目编号:21YF5FA129,22YF7FG188)
甘肃省自然科学基金项目(项目编号:22JR5RG567)
甘肃省科技计划项目基础研究计划(项目编号:22JR11RG222)。