{"title":"分裂突变体可防止突变体缺陷大肠杆菌的突变表型。","authors":"Hiroyuki Kamiya","doi":"10.1186/s41021-024-00314-8","DOIUrl":null,"url":null,"abstract":"<p><strong>Background: </strong>The Escherichia coli MutT (NudA) protein catalyzes the hydrolysis of an oxidized form of dGTP, 8-oxo-7,8-dihydro-dGTP (8-hydroxy-dGTP), and the spontaneous mutation frequency is elevated in E. coli cells deficient in the mutT gene.</p><p><strong>Results: </strong>A split MutT, comprising the N-terminal (residues 1-95) and C-terminal (residues 96-129) peptides, was designed based on the known tertiary structure and linker insertion mutagenesis experiments. The mutator phenotype was complemented when the two peptides were separately expressed in mutT E. coli cells.</p><p><strong>Conclusions: </strong>These results indicated that this split MutT functions as a nucleotide pool sanitization enzyme in vivo.</p>","PeriodicalId":12709,"journal":{"name":"Genes and Environment","volume":"46 1","pages":"19"},"PeriodicalIF":2.7000,"publicationDate":"2024-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11460165/pdf/","citationCount":"0","resultStr":"{\"title\":\"Split MutT prevents the mutator phenotype of mutT-deficient Escherichia coli.\",\"authors\":\"Hiroyuki Kamiya\",\"doi\":\"10.1186/s41021-024-00314-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><strong>Background: </strong>The Escherichia coli MutT (NudA) protein catalyzes the hydrolysis of an oxidized form of dGTP, 8-oxo-7,8-dihydro-dGTP (8-hydroxy-dGTP), and the spontaneous mutation frequency is elevated in E. coli cells deficient in the mutT gene.</p><p><strong>Results: </strong>A split MutT, comprising the N-terminal (residues 1-95) and C-terminal (residues 96-129) peptides, was designed based on the known tertiary structure and linker insertion mutagenesis experiments. The mutator phenotype was complemented when the two peptides were separately expressed in mutT E. coli cells.</p><p><strong>Conclusions: </strong>These results indicated that this split MutT functions as a nucleotide pool sanitization enzyme in vivo.</p>\",\"PeriodicalId\":12709,\"journal\":{\"name\":\"Genes and Environment\",\"volume\":\"46 1\",\"pages\":\"19\"},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2024-10-08\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11460165/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Genes and Environment\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.1186/s41021-024-00314-8\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"GENETICS & HEREDITY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Genes and Environment","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1186/s41021-024-00314-8","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"GENETICS & HEREDITY","Score":null,"Total":0}
引用次数: 0
摘要
背景:大肠杆菌MutT(NudA)蛋白催化dGTP的一种氧化形式--8-氧代-7,8-二氢-dGTP(8-羟基-dGTP)的水解,在缺乏mutT基因的大肠杆菌细胞中,自发突变频率升高:结果:根据已知的三级结构和连接体插入诱变实验,设计了一个由 N 端(残基 1-95)和 C 端(残基 96-129)多肽组成的分裂 MutT。在 mutT 大肠杆菌细胞中分别表达这两种肽时,突变体表型得到了补充:这些结果表明,这种分裂的 MutT 在体内具有核苷酸池消毒酶的功能。
Split MutT prevents the mutator phenotype of mutT-deficient Escherichia coli.
Background: The Escherichia coli MutT (NudA) protein catalyzes the hydrolysis of an oxidized form of dGTP, 8-oxo-7,8-dihydro-dGTP (8-hydroxy-dGTP), and the spontaneous mutation frequency is elevated in E. coli cells deficient in the mutT gene.
Results: A split MutT, comprising the N-terminal (residues 1-95) and C-terminal (residues 96-129) peptides, was designed based on the known tertiary structure and linker insertion mutagenesis experiments. The mutator phenotype was complemented when the two peptides were separately expressed in mutT E. coli cells.
Conclusions: These results indicated that this split MutT functions as a nucleotide pool sanitization enzyme in vivo.
期刊介绍:
Genes and Environment is an open access, peer-reviewed journal that aims to accelerate communications among global scientists working in the field of genes and environment. The journal publishes articles across a broad range of topics including environmental mutagenesis and carcinogenesis, environmental genomics and epigenetics, molecular epidemiology, genetic toxicology and regulatory sciences.
Topics published in the journal include, but are not limited to, mutagenesis and anti-mutagenesis in bacteria; genotoxicity in mammalian somatic cells; genotoxicity in germ cells; replication and repair; DNA damage; metabolic activation and inactivation; water and air pollution; ROS, NO and photoactivation; pharmaceuticals and anticancer agents; radiation; endocrine disrupters; indirect mutagenesis; threshold; new techniques for environmental mutagenesis studies; DNA methylation (enzymatic); structure activity relationship; chemoprevention of cancer; regulatory science. Genetic toxicology including risk evaluation for human health, validation studies on testing methods and subjects of guidelines for regulation of chemicals are also within its scope.