Chlorella virus pyrimidine dimer glycosylase and Escherichia coli endonucleases IV and V have incision activity on 2, 2, 4-triamino-5(2H)-oxazolone. (December 2015)

• Record Type: Journal Article
• Authors: Kino, Katsuhito; Suzuki, Masayo; Morikawa, Masayuki; Kobayashi, Takanobu; Iwai, Shigenori; Miyazawa, Hiroshi
• Is Part Of: Genes and environment. Volume 37:Number 1(2015)
• Page Start: 1
• Page End: 6
• Publication Date: 2015-12
• Subjects: Guanine oxidation -- Oxazolone -- Chlorella virus pyrimidine dimer glycosylase -- Escherichia coli endonucleases IV -- Escherichia coli endonucleases V; Mutagenesis -- Periodicals; Pollution -- Environmental aspects -- Periodicals; Mutagens -- Periodicals; Mutation (Biology) -- Periodicals; Genetic toxicology -- Periodicals; Genetic toxicology; Mutagenesis; Mutagens; Mutation (Biology); Pollution -- Environmental aspects; Periodicals; 572.838
• DOI: 10.1186/s41021-015-0022-8
• Languages: English
• ISSNs: 1880-7062

Abstract

Abstract Introduction 2, 2, 4-Triamino-5(2H )-oxazolone (Oz) in a DNA strand is an oxidation product of guanine and 8-oxo-7, 8-dihydroguanine, and such a lesion can cause G-to-C transversions. Previously, Fpg/Nei and Nth were shown to have incision activity on Oz. Findings We investigated the activities of chlorella virus pyrimidine dimer glycosylase (cvPDG) andEscherichia coli endonucleases IV (Nfo) and V (Nfi) on Oz. Although the three enzymes have different repair mechanisms from Fpg/Nei and Nth, they still had incision activity on Oz. Conclusions Given the incision activities of cvPDG, Nfo and Nfi on Oz in addition to Fpg/Nei and Nth, Oz is DNA damage that can be repaired by diverse enzymes.