The H2TH-like motif of the Escherichia coli multifunctional protein KsgA is required for DNA binding involved in DNA repair and the suppression of mutation frequencies
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- 資料種別
- 記事
- 著者・編者
- Yuichiro HayashiMasafumi FunakoshiKaname Hirosawa
- 出版年月日等
- 2023-04-12
- 出版年（W3CDTF）
- 2023-04-12
- タイトル（掲載誌）
- Genes and environment
- 巻号年月日等（掲載誌）
- 45(13)
- 掲載巻
- 45(13)
- ISSN（掲載誌）
- 1880-7062
- ISSN-L（掲載誌）
- 1880-7046
- 本文の言語コード
- eng
- DOI
- 10.1186/s41021-023-00266-5
- 国立国会図書館永続的識別子
- info:ndljp/pid/12998764
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- コレクション（個別）
- 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > その他
- 収集根拠
- オンライン資料収集制度
- 受理日（W3CDTF）
- 2023-09-27T15:09:56+09:00
- 保存日（W3CDTF）
- 2023-09-27
- 記録形式（IMT）
- application/pdf
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- 国立国会図書館内限定公開
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- info:ndljp/pid/12998751
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- 国立国会図書館 : 国立国会図書館デジタルコレクション
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- [Background] DNA oxidatively damaged by reactive oxygen species is repaired by base excision repair (BER) pathway proteins, with DNA glycosylases removing damaged or mismatched bases in the first step of BER. KsgA is a multifunctional protein that exhibits the activities of two enzymes, DNA glycosylase and rRNA dimethyltransferase. The structure-function relationship of the KsgA protein in cellular DNA repair remains unclear because the domains required for KsgA to recognize DNA have not been identified. [Purpose] To clarify the mechanisms by which KsgA recognizes damaged DNA and to identify the DNA-binding site, which exists in KsgA. [Methods] A structural analysis and in vitro DNA-protein binding assay were performed. The C-terminal function of the KsgA protein was investigated in vitro and in vivo. [Results] The 3D conformations of KsgA, MutM, and Nei were compared at UCSF Chimera. The root mean square deviation of KsgA (214-273) and MutM (148-212) and that of KsgA (214-273) and Nei (145-212) were 1.067 and 1.188 Å, both less than 2 Å, suggesting that the C terminal of KsgA is spatially similar to the H2TH domains of MutM and Nei. The full-length KsgA protein and KsgA lacking 1-8 or 214-273 amino acids were purified and used in gel mobility shift assays. KsgA exhibited DNA-binding activity, which was lost in the C-terminally deleted KsgA protein. Spontaneous mutation frequency was measured using a mutM mutY ksgA-deficient strain, and the results obtained showed that the mutation frequency was not suppressed by KsgA lacking the C-terminal region, whereas it was in KsgA. To assess dimethyltransferase activity, kasugamycin sensitivity was assessed in wild-type and ksgA-deficient strains. Plasmids carrying the full-length ksgA gene and C-terminal deletion gene were introduced into ksgA-deficient strains. KsgA lacking the C terminus restored dimethyltransferase activity in the ksgA-deficient strain as well as KsgA. [Conclusion] The present results confirmed that one enzyme exhibited two activities and revealed that the C-terminal (214-273) amino acids of KsgA were highly similar to the H2TH structural domain, exhibited DNA-binding activity, and inhibited spontaneous mutations. This site is not essential for dimethyltransferase activity.
- DOI
- 10.1186/s41021-023-00266-5
- オンライン閲覧公開範囲
- インターネット公開
- 著作権情報
- © The Author(s) 2023.This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
- 関連情報（URI）
- 参照
- Characterization of Escherichia coli Endonuclease VIIIKasugamycin resistant mutants of Bacillus stearothermophilus lacking the enzyme for the methylation of two adjacent adenosines in 16S ribosomal RNAThe Biochemical Role of the Human NEIL1 and NEIL3 DNA Glycosylases on Model DNA Replication ForksEukaryotic endonuclease VIII-Like proteins: New components of the base excision DNA repair systemImplication of Mammalian Ribosomal Protein S3 in the Processing of DNA DamageChange in Methylation of 16S Ribosomal RNA Associated with Mutation to Kasugamycin Resistance in Escherichia coliMutations induced by 5-formyl-2′-deoxyuridine in Escherichia coli include base substitutions that can arise from mispairs of 5-formyluracil with guanine, cytosine and thymineCloning and Characterization of theKlDIM1 Gene fromKluyveromyces lactis Encoding the m26A Dimethylase of the 18S rRNAFocus on DNA Glycosylases—A Set of Tightly Regulated Enzymes with a High Potential as Anticancer Drug Targets16S rRNA methyltransferase KsgA contributes to oxidative stress resistance and virulence in Staphylococcus aureusKsgA, a 16S rRNA adenine methyltransferase, has a novel DNA glycosylase/AP lyase activity to prevent mutations in Escherichia coliMutagenicity, toxicity and repair of DNA base damage induced by oxidationSubstrate and Mispairing Properties of 5-Formyl-2'-Deoxyuridine 5'-Triphosphate Assessed by in vitro DNA Polymerase ReactionsRibosomal protein S3 associates with the TFIIH complex and positively regulates nucleotide excision repairCatalytic Mechanism of <i>Escherichia coli</i> Endonuclease VIII: Roles of the Intercalation Loop and the Zinc FingerNH2-terminal Proline Acts as a Nucleophile in the Glycosylase/AP-Lyase Reaction Catalyzed by Escherichia coli Formamidopyrimidine-DNA Glycosylase (Fpg) ProteinNucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNAIdentification of high excision capacity for 5-hydroxymethyluracil mispaired with guanine in DNA of Escherichia coli MutM, Nei and Nth DNA glycosylasesThe Catalytic Mechanism of Fpg ProteinThe Fpg/Nei Family of DNA GlycosylasesChloroplast Development at Low Temperatures Requires a Homolog of <i>DIM1</i>, a Yeast Gene Encoding the 18S rRNA DimethylaseInhibition of Escherichia coli RecA coprotease activities by DinINew substrates for old enzymes. 5-Hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase.Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, <i>Thermus thermophilus</i> HB8Reverse chemical mutagenesis: identification of the mutagenic lesions resulting from reactive oxygen species-mediated damage to DNA.The DIM1 Gene Responsible for the Conserved m62Am62A Dimethylation in the 3′-Terminal Loop of 18 S rRNA is Essential in YeastRecognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolutionBiological consequences of free radical-damaged DNA bases1,2 1Guest Editor: Miral Dizdaroglu 2This article is part of a series of reviews on “Oxidative DNA Damage and Repair.” The full list of papers may be found on the homepage of the journal.Dissection of 16S rRNA Methyltransferase (KsgA) Function in <i>Escherichia coli</i>Mechanism of Kasugamycin Resistance in Escherichia coliBase Excision RepairHuman mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loopEscherichia coli endonuclease VIII: cloning, sequencing, and overexpression of the nei structural gene and characterization of nei and nei nth mutantsThe mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivoOxidative damage to DNA: formation, measurement and biochemical featuresOxidants, antioxidants, and the degenerative diseases of aging.The enigma of endonuclease VIIIDimethyl Adenosine Transferase (KsgA) Deficiency in Salmonella enterica Serovar Enteritidis Confers Susceptibility to High Osmolarity and Virulence Attenuation in ChickensHuman DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNASubstrate specificity of the Escherichia coli Fpg protein formamidopyrimidine-DNA glycosylase: excision of purine lesions in DNA produced by ionizing radiation or photosensitizationDrosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activityStructure of a Duplex DNA Containing a Thymine Glycol Residue in SolutionIdentification of Repair Enzymes for 5-Formyluracil in DNAA novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIIIBase-excision repair of oxidative DNA damage by DNA glycosylasesMajor oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing<i>in vitro</i>Hide and seek: How do DNA glycosylases locate oxidatively damaged DNA bases amidst a sea of undamaged bases?Characterization of the ksgA gene of Escherichia coli determining kasugamycin sensitivity8-oxoguanine (8-hydroxyguanine) DNA glycosylase and its substrate specificity.Significance of error‐avoiding mechanisms for oxidative DNA damage in carcinogenesis
- 連携機関・データベース
- 国立情報学研究所 : CiNii Research
- 提供元機関・データベース
- 学術機関リポジトリデータベース雑誌記事索引データベースCrossref科学研究費助成事業データベース科学研究費助成事業データベース
- 書誌ID（NDLBibID）
- 12998764