Adenine Glycosylase MutY of Corynebacterium pseudotuberculosis presents the antimutator phenotype and evidences of glycosylase/AP lyase activity in vitro

Faria, Rafael Cançado de; Vila-Nova, Liliane Gonçalves; Bitar, Mainá; Resende, Bruno Carvalho; Arantes, Larissa Sousa; Rebelato, Arnaldo Basso; Azevedo, Vasco; Franco, Glória Regina; Machado, Carlos Renato; Santos, Luciana Lara dos; Lopes, Débora de Oliveira

doi:10.1016/j.meegid.2016.07.028

Cited by 6 publications

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“…24,25 Among the enzymes involved in DNA repair, the helix−hairpin−helix DNA glycosylase (HhH-DG) superfamily can target and repair DNA lesions with high diversity. 26,27 The defining feature of the HhH-DG superfamily is a highly conserved HhH motif followed by a Gly/Pro-rich loop and a conserved Asp residue (HhH-GPD motif). 26 The T h i s c o n t e n t i s HhH motif is widespread in DNA-binding proteins and has been proved to be the pivotal structure for DNA binding.…”

Section: Introductionmentioning

confidence: 99%

“…Even with the high precision of the polymerase during DNA replication, there is still a chance (10 –8 –10 –6 ) for each base to be replicated incorrectly at each copy, resulting in the DNA mismatch. A series of enzymes related to DNA mismatch repair (MMR) emerge during biological evolution to correct these errors. , Among the enzymes involved in DNA repair, the helix–hairpin–helix DNA glycosylase (HhH-DG) superfamily can target and repair DNA lesions with high diversity. , The defining feature of the HhH-DG superfamily is a highly conserved HhH motif followed by a Gly/Pro-rich loop and a conserved Asp residue (HhH-GPD motif) . The HhH motif is widespread in DNA-binding proteins and has been proved to be the pivotal structure for DNA binding. , …”

Section: Introductionmentioning

confidence: 99%

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Functionalization of Mesoporous Silica with a G-A-Mismatched dsDNA Chain for Efficient Identification and Selective Capturing of the MutY Protein

Sun

Wang

Chen

2023

ACS Appl. Mater. Interfaces

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MUTYH adenine DNA glycosylase and its homologous protein (collectively MutY) are typical DNA glycosylases with a [4Fe4S] cluster and a helix–hairpin–helix (HhH) motif in its structure. In the present work, the binding behaviors of the MutY protein to dsDNA containing different base mismatches were investigated. The type and distribution of base mismatch in the dsDNA chain were found to influence the DNA–protein binding interaction greatly. The [4Fe4S] cluster of the MutY protein is able to identify a G-A mismatch in the dsDNA chain specifically by monitoring the anomalies of charge transport in the dsDNA chain, allowing the entrance of the identified dsDNA chain into the internal cavity of the MutY protein and the strong DNA–protein binding at the HhH motif of the protein through multiple H-bonds. The dsDNA chain with a centrally located G-A mismatch is thus functionalized on mesoporous silica (MSN) via amination reaction, and the obtained dsDNA(G-A)@MSN is used as a powerful sorbent for the selective capturing of the MutY protein from complex samples. By using 0.5% NH3·H2O (m/v) as a stripping reagent, efficient isolation of the MutY protein from different cell lines and bacteria is achieved and the recovered MutY protein is demonstrated to maintain favorable DNA adenine glycosylase activity.

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