scholarly journals Mutation Spectrum Induced by 8-Bromoguanine, a Base Damaged by Reactive Brominating Species, in Human Cells

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Kazuya Shinmura ◽  
Hisami Kato ◽  
Masanori Goto ◽  
Hong Tao ◽  
Yusuke Inoue ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Shuttle Vector ◽  
Human Cells ◽  
Dna Glycosylase ◽  
Repair System ◽  
Dna Glycosylases ◽  
Dna Cleavage Activity ◽  
Base Lesion ◽  
Mutation Assay ◽  
Forward Mutation

To date, the types of mutations caused by 8-bromoguanine (8BrG), a major base lesion induced by reactive brominating species during inflammation, in human cells and the 8BrG repair system remain largely unknown. In this study, we performed a supF forward mutation assay using a shuttle vector plasmid containing a single 8BrG in three kinds of human cell lines and revealed that 8BrG in DNA predominantly induces a G → T mutation but can also induce G → C, G → A, and delG mutations in human cells. Next, we tested whether eight kinds of DNA glycosylases (MUTYH, MPG, NEIL1, OGG1, SMUG1, TDG, UNG2, and NTHL1) are capable of repairing 8BrG mispairs with any of the four bases using a DNA cleavage activity assay. We found that both the SMUG1 protein and the TDG protein exhibit DNA glycosylase activity against thymine mispaired with 8BrG and that the MUTYH protein exhibits DNA glycosylase activity against adenine mispaired with 8BrG. These results suggest that 8BrG induces some types of mutations, chiefly a G → T mutation, in human cells, and some DNA glycosylases are involved in the repair of 8BrG.

scholarly journals A ‘new lease of life’: FnCpf1 possesses DNA cleavage activity for genome editing in human cells

2017 ◽  
Vol 45 (19) ◽  
pp. 11295-11304 ◽  
Author(s):  
Mengjun Tu ◽  
Li Lin ◽  
Yilu Cheng ◽  
Xiubin He ◽  
Huihui Sun ◽  
...  
Keyword(s):  
Genome Editing ◽  
Dna Cleavage ◽  
Human Cells ◽  
Cleavage Activity ◽  
Dna Cleavage Activity

DNA-cleavage activity of the iron(II) complex with optically active ligands, meta- and para-xylyl-linked N’,N’-dipyridylmethyl-cyclohexane-1,2-diamine

2021 ◽  
Vol 36 ◽  
pp. 127834
Author(s):  
Koichi Kato ◽  
Yoshimi Ichimaru ◽  
Yoshinori Okuno ◽  
Yoshihiro Yamaguchi ◽  
Wanchun Jin ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Optically Active ◽  
Cleavage Activity ◽  
Dna Cleavage Activity

scholarly journals A YoeB toxin cleaves both RNA and DNA

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Julia McGillick ◽  
Jessica R. Ames ◽  
Tamiko Murphy ◽  
Christina R. Bourne
Keyword(s):  
Dna Cleavage ◽  
Divalent Cations ◽  
Nuclease Activity ◽  
Dose Dependence ◽  
Cleavage Activity ◽  
Double Stranded Dna ◽  
Dna Cleavage Activity ◽  
Evolutionarily Conserved ◽  
Toxin Protein ◽  
Rna And Dna

AbstractType II toxin-antitoxin systems contain a toxin protein, which mediates diverse interactions within the bacterial cell when it is not bound by its cognate antitoxin protein. These toxins provide a rich source of evolutionarily-conserved tertiary folds that mediate diverse catalytic reactions. These properties make toxins of interest in biotechnology applications, and studies of the catalytic mechanisms continue to provide surprises. In the current work, our studies on a YoeB family toxin from Agrobacterium tumefaciens have revealed a conserved ribosome-independent non-specific nuclease activity. We have quantified the RNA and DNA cleavage activity, revealing they have essentially equivalent dose-dependence while differing in requirements for divalent cations and pH sensitivity. The DNA cleavage activity is as a nickase for any topology of double-stranded DNA, as well as cleaving single-stranded DNA. AtYoeB is able to bind to double-stranded DNA with mid-micromolar affinity. Comparison of the ribosome-dependent and -independent reactions demonstrates an approximate tenfold efficiency imparted by the ribosome. This demonstrates YoeB toxins can act as non-specific nucleases, cleaving both RNA and DNA, in the absence of being bound within the ribosome.

scholarly journals Correction to Copper(II) Complexes of l-Arginine as Netropsin Mimics Showing DNA Cleavage Activity in Red Light

2019 ◽  
Vol 58 (19) ◽  
pp. 13502-13503
Author(s):  
Ashis K. Patra ◽  
Tuhin Bhowmick ◽  
Sovan Roy ◽  
Suryanarayanarao Ramakumar ◽  
Akhil R. Chakravarty
Keyword(s):  
Dna Cleavage ◽  
Red Light ◽  
Cleavage Activity ◽  
Dna Cleavage Activity

Cytotoxic copper (II) mixed ligand complexes: Crystal structure and DNA cleavage activity

2011 ◽  
Vol 46 (9) ◽  
pp. 4537-4547 ◽  
Author(s):  
Verasuntharam M. Manikandamathavan ◽  
Royapuram P. Parameswari ◽  
Thomas Weyhermüller ◽  
Hannah R. Vasanthi ◽  
Balachandran Unni Nair
Keyword(s):  
Crystal Structure ◽  
Dna Cleavage ◽  
Mixed Ligand ◽  
Mixed Ligand Complexes ◽  
Cleavage Activity ◽  
Dna Cleavage Activity

The effect of sequence context on the activity of cytosine DNA glycosylases

2015 ◽  
Vol 11 (12) ◽  
pp. 3273-3278
Author(s):  
Scott T. Kimber ◽  
Tom Brown ◽  
Keith R. Fox
Keyword(s):  
Dna Glycosylase ◽  
Dna Glycosylases ◽  
Sequence Context ◽  
Uracil Dna Glycosylase

We have examined how sequence context affects the ability of (N204D:L272A) mutants of uracil DNA glycosylase to cleave CX mismatches.

A novel bacterial reversion and forward mutation assay based on green fluorescent protein

1998 ◽  
Vol 414 (1-3) ◽  
pp. 95-105 ◽  
Author(s):  
Neal F Cariello ◽  
Sabrina Narayanan ◽  
Puntipa Kwanyuen ◽  
Heidi Muth ◽  
Warren M Casey
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Green Fluorescent ◽  
Mutation Assay ◽  
Forward Mutation

scholarly journals The TREX2 3′→ 5′ Exonuclease Physically Interacts with DNA Polymerase δ and Increases Its Accuracy

2002 ◽  
Vol 2 ◽  
pp. 275-281 ◽  
Author(s):  
Igor V. Shevelev ◽  
Kristijan Ramadan ◽  
Ulrich Hubscher
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Error Rates ◽  
High Fidelity ◽  
Replication Machinery ◽  
Dna Polymerase Δ ◽  
Pol I ◽  
Calf Thymus ◽  
Mutation Assay ◽  
Forward Mutation

Proofreading function by the 3′→ 5′ exonuclease of DNA polymerase δ (pol δ) is consistent with the observation that deficiency of the associated exonuclease can lead to a strong mutation phenotype, high error rates during DNA replication, and ultimately cancer. We have isolated pol δdfrom isotonic (pol δi) and detergent (pol δd) calf thymus extracts. Pol δdhad a 20-fold higher ratio of exonuclease to DNA polymerase than pol δi. This was due to the physical association of the TREX2 exonuclease to pol δd, which was missing from pol δi. Pol δdwas fivefold more accurate than pol δiunder error-prone conditions (1 μM dGTP and 20 dATP, dCTP, and dTTP) in a M13mp2 DNA forward mutation assay, and fourfold more accurate in an M13mp2T90 reversion assay. Under error-free conditions (20 μM each of the four dNTPs), however, both polymerases showed equal fidelity. Our data suggested that autonomous 3′→ 5′ exonucleases, such as TREX2, through its association with pol I can guarantee high fidelity under difficult conditions in the cell (e.g., imbalance of dNTPs) and can add to the accuracy of the DNA replication machinery, thus preventing mutagenesis.

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