{"title":"DNA Repair and Mutagenesis of ADP-Ribosylated DNA by Pierisin","authors":"Masanobu Kawanishi, Takashi Yagi, Yukari Totsuka, Keiji Wakabayashi","doi":"10.3390/toxins16080331","DOIUrl":null,"url":null,"abstract":"Pierisin is a DNA-targeting ADP-ribosyltransferase found in cabbage white butterfly (Pieris rapae). Pierisin transfers an ADP-ribosyl moiety to the 2-amino group of the guanine residue in DNA, yielding N2-(ADP-ribos-1-yl)-2′-deoxyguanosine (N2-ADPR-dG). Generally, such chemically modified DNA is recognized as DNA damage and elicits cellular responses, including DNA repair pathways. In Escherichia coli and human cells, it has been experimentally demonstrated that N2-ADPR-dG is a substrate of the nucleotide excision repair system. Although DNA repair machineries can remove most lesions, some unrepaired damages frequently lead to mutagenesis through DNA replication. Replication past the damaged DNA template is called translesion DNA synthesis (TLS). In vitro primer extension experiments have shown that eukaryotic DNA polymerase κ is involved in TLS across N2-ADPR-dG. In many cases, TLS is error-prone and thus a mutagenic process. Indeed, the induction of G:C to T:A and G:C to C:G mutations by N2-ADPR-dG in the hypoxanthine phosphoribosyltransferase gene mutation assay with Chinese hamster cells and supF shuttle vector plasmids assay using human fibroblasts has been reported. This review provides a detailed overview of DNA repair, TLS and mutagenesis of N2-ADPR-dG induced by cabbage butterfly pierisin-1.","PeriodicalId":23119,"journal":{"name":"Toxins","volume":null,"pages":null},"PeriodicalIF":3.9000,"publicationDate":"2024-07-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Toxins","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.3390/toxins16080331","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Pierisin is a DNA-targeting ADP-ribosyltransferase found in cabbage white butterfly (Pieris rapae). Pierisin transfers an ADP-ribosyl moiety to the 2-amino group of the guanine residue in DNA, yielding N2-(ADP-ribos-1-yl)-2′-deoxyguanosine (N2-ADPR-dG). Generally, such chemically modified DNA is recognized as DNA damage and elicits cellular responses, including DNA repair pathways. In Escherichia coli and human cells, it has been experimentally demonstrated that N2-ADPR-dG is a substrate of the nucleotide excision repair system. Although DNA repair machineries can remove most lesions, some unrepaired damages frequently lead to mutagenesis through DNA replication. Replication past the damaged DNA template is called translesion DNA synthesis (TLS). In vitro primer extension experiments have shown that eukaryotic DNA polymerase κ is involved in TLS across N2-ADPR-dG. In many cases, TLS is error-prone and thus a mutagenic process. Indeed, the induction of G:C to T:A and G:C to C:G mutations by N2-ADPR-dG in the hypoxanthine phosphoribosyltransferase gene mutation assay with Chinese hamster cells and supF shuttle vector plasmids assay using human fibroblasts has been reported. This review provides a detailed overview of DNA repair, TLS and mutagenesis of N2-ADPR-dG induced by cabbage butterfly pierisin-1.
Pierisin 是一种 DNA 靶向 ADP 核糖基转移酶,存在于卷心菜白蝶(Pieris rapae)中。Pierisin 能将 ADP-核糖基分子转移到 DNA 中鸟嘌呤残基的 2-氨基上,生成 N2-(ADP-核糖-1-基)-2′-脱氧鸟苷(N2-ADPR-dG)。一般来说,这种经过化学修饰的 DNA 被认为是 DNA 损伤,会引起细胞反应,包括 DNA 修复途径。在大肠杆菌和人类细胞中,实验证明 N2-ADPR-dG 是核苷酸切除修复系统的底物。尽管 DNA 修复机制可以清除大多数病变,但一些未修复的损伤经常会通过 DNA 复制导致突变。通过受损 DNA 模板进行的复制称为转座子 DNA 合成(TLS)。体外引物延伸实验表明,真核生物 DNA 聚合酶 κ 参与了跨 N2-ADPR-dG 的 TLS。在许多情况下,TLS 容易出错,因此是一个诱变过程。事实上,在用中国仓鼠细胞进行的次黄嘌呤磷酸核糖转移酶基因突变试验和用人成纤维细胞进行的 supF 穿梭载体质粒试验中,N2-ADPR-dG 都诱导了 G:C 到 T:A 和 G:C 到 C:G 的突变。本综述详细概述了甘蓝蝴蝶穿刺素-1 诱导的 DNA 修复、TLS 和 N2-ADPR-dG 诱变。
期刊介绍:
Toxins (ISSN 2072-6651) is an international, peer-reviewed open access journal which provides an advanced forum for studies related to toxins and toxinology. It publishes reviews, regular research papers and short communications. Our aim is to encourage scientists to publish their experimental and theoretical results in as much detail as possible. There is no restriction on the length of the papers. The full experimental details must be provided so that the results can be reproduced.