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食品研究与开发:2024,45(20):191-201
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基于比较基因组学的红曲霉VeA、VelB生物信息学分析
(1.塔里木大学食品科学与工程学院南疆特色农产品深加工兵团重点实验室,新疆 阿拉尔 843300;2.武汉轻工大学食品科学与工程学院,湖北 武汉 430048;3.华中农业大学传统发酵食品湖北国际科技合作基地,湖北 武汉 430070)
Bioinformatics Analysis of Monascus VeA and VelB Based on Comparative Genomics
(1.Key Laboratory of Special Agricultural Products Further Processing in Southern Xinjiang of Xinjiang Production and Construction Corps,College of Food Science and Engineering,Tarim University,Alar 843300,Xinjiang,China;2.School of Food Science and Engineering,Wuhan Polytechnic University,Wuhan 430048,Hubei,China;3.Hubei International Science and Technology Cooperation Base of Traditional Fermented Food,Huazhong Agricultural University,Wuhan 430070,Hubei,China)
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投稿时间:2023-03-29    
中文摘要: 红曲霉(Monascus spp.)是一种可产生红曲色素(monascus pigments,MPs)、莫纳可林K(moncolin K,MK)、γ-氨基丁酸(γ-aminobutyric acid,GABA)等多种有益代谢产物的工业用重要生产菌种。该文对4 株高产红色素的红曲霉(M7、NRRL 1597、NRRL 1596、YY-1)全局调控因子VeA、VelB 进行基因组学分析。结果表明:4 株红曲霉VeA 基因编码的蛋白均含有1 个天鹅绒(velvet)结构域、核定位信号(nuclear localization signal,NLS)和不稳定的富脯氨酸区域(proline-,glutamic acid-,serine-,and threonine-rich sequence,PEST);VelB 基因编码的蛋白含有2 个velvet 结构域,不含NLS 区域。VeA 蛋白与典型丝状真菌的VeA 蛋白相似度为37.4%~62.5%;红曲霉VelB 蛋白与典型丝状真菌相似度为51.2%~84.1%,这说明红曲霉VeA 蛋白和VelB 蛋白具有类似于其它丝状真菌的功能。红曲霉VeA 蛋白、VelB 蛋白的一级结构主要由脯氨酸和丝氨酸组成,不含明显跨膜结构域和信号肽;红曲霉VeA 蛋白主要位于细胞核内,VelB 蛋白在细胞核和细胞质均有分布;VeA 蛋白和VelB 蛋白均具有多个丝氨酸、苏氨酸和酪氨酸激酶磷酸化位点;VeA 蛋白二级结构主要为β-折叠和无规则卷曲结构,VelB 蛋白主要为α-螺旋、β-折叠和无规则卷曲结构;红曲霉VeA 蛋白、VelB 蛋白三级结构模型与典型丝状真菌VeA 蛋白、VelB 蛋白三级结构模型相似,蛋白相互作用网络预测VeA 蛋白和VelB 蛋白间可以相互作用。上述分析结果推测红曲霉VeA 蛋白、VelB 蛋白的功能及作用机理可能与其它真菌相似,具有调控菌株的生长发育、次级代谢等功能。
Abstract:Monascus spp. are important industrial microorganisms that can produce beneficial metabolites such as monascus pigments(MPs),moncolin K(MK),and gamma-aminobutyric acid(GABA). The genomic analysis was carried out for the global regulatory factor genes VeA and VelB of four Monascus strains(M7,NRRL 1597,NRRL 1596,and YY-1)with high production of red pigment. The results showed that the proteins encoded by VeA in the four strains contained a velvet domain,a nuclear localization signal(NLS),and a proline-,glutamic acid-,serine-,and threonine-rich(PEST)sequence.The protein encoded by VelB contained two velvet domains but lacked an NLS region. The similarity of VeA and VelB sequences between Monascus and typical filamentous fungi was within the ranges of 37.4%-62.5% and 51.2%-84.1%,respectively. This suggested that VeA and VelB in Monascus had similar functions to those in other filamentous fungi. The primary structures of Monascus VeA and VelB were mainly composed of proline and serine,with no obvious transmembrane structure or signal peptide. Monascus VeA was mainly located in the nucleus,while VelB existed in both the nucleus and cytoplasm.Both proteins had multiple serine,threonine,and tyrosine kinase phosphorylation sites. The secondary structure of Monascus VeA was mainly composed of beta-sheets and random coils,while that of Monascus VelB was mainly composed of alpha-helices,beta-sheets,and random coils. The threedimensional structures of VeA and VelB in Monascus were similar to those in typical filamentous fungi. The protein-protein interaction network showcased that VeA and VelB interacted with each other. The results suggested that the functions and mechanisms of VeA and VelB in Monascus were similar to those in other fungi,and the two proteins might be involved in regulating the growth,development,and secondary metabolism of strains.
文章编号:202420024     中图分类号:    文献标志码:
基金项目:国家自然科学基金地区基金项目(32060526);兵团财政科技计划(2021CB023);第三师图木舒克市科技计划项目(KY2021GG18)
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