Peroxidase from proso millet exhibits endonuclease-like activity

2019 ◽  
Vol 51 (7) ◽  
pp. 688-696 ◽  
Author(s):  
Xiaodong Cui ◽  
Tingfen Wang ◽  
Wenming Wang ◽  
Hongfei Wang ◽  
Zhuanhua Wang
Keyword(s):  
Dna Cleavage ◽  
Heme Proteins ◽  
Hydrolytic Cleavage ◽  
Oxygen Species ◽  
Linear Forms ◽  
Circular Dna ◽  
Proso Millet ◽  
Cleavage Activity ◽  
Phosphodiester Bonds ◽  
Dna Cleavage Activity

Abstract In this study, the mechanism of DNA cleavage by cationic peroxidase from proso millet (PmPOD) was investigated. PmPOD cleaved supercoiled circular DNA into both nicked circular and linear forms via a cleavage mechanism that resembles those of native endonucleases. Inhibition and ligation studies demonstrated that reactive oxygen species and the ferriprotoporphyrin IX moiety in PmPOD are not involved in PmPOD-mediated DNA cleavage. Similar to other endonucleases, Mg ions considerably enhance the DNA cleavage activity of PmPOD. Further studies suggested that PmPOD can disrupt phosphodiester bonds in DNA and mononucleotides, indicating that it is a phosphatase. The phosphatase activity of PmPOD is higher than that of horseradish peroxidase (HRP), but the peroxidase activity of PmPOD was lower than that of HRP. PmPOD-mediated hydrolytic cleavage of DNA observed in this study is different from those reported for heme proteins. This study provides valuable insights into the distinct mechanisms underlying DNA cleavage by heme proteins.

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

Extra Copper-mediated Enhancement of the DNA Cleavage Activity Supported with Wild-type Cu, Zn Superoxide Dismutase

2008 ◽  
Vol 26 (3) ◽  
pp. 564-570 ◽  
Author(s):  
Ruo-Yu ZHOU ◽  
Wei JIANG ◽  
Li-Na ZHANG ◽  
Li WANG ◽  
Chang-Lin LIU
Keyword(s):  
Superoxide Dismutase ◽  
Dna Cleavage ◽  
Wild Type ◽  
Cleavage Activity ◽  
Dna Cleavage Activity

A rapid synthesis of 2-((2-amino-4,6-dimethylpyrimidine-5yl)diazenyl)benzoic acid: Experimental, DFT study and DNA cleavage activity

2018 ◽  
Vol 1171 ◽  
pp. 906-914 ◽  
Author(s):  
Çiğdem Karabacak Atay ◽  
Fatih Duman ◽  
Merve Gökalp ◽  
Tahir Tilki ◽  
Sevgi Ozdemir Kart
Keyword(s):  
Benzoic Acid ◽  
Dna Cleavage ◽  
Dft Study ◽  
Rapid Synthesis ◽  
Cleavage Activity ◽  
Dna Cleavage Activity

Spectral analysis of radical metalloenzyme using EPR in Hydrolases

2021 ◽  
Vol 25 (11) ◽  
pp. 132-137
Author(s):  
Pramod Sonawane
Keyword(s):  
Dna Cleavage ◽  
Mixed Valence ◽  
Reduced Form ◽  
Electron Interaction ◽  
Coupling Constant ◽  
Epr Spectrum ◽  
Cleavage Activity ◽  
Dna Cleavage Activity ◽  
Sample Spectrum ◽  
Radical Signal

One of the categories of hydrolase is acid phosphatase which is isolated from sweet potato (spAP). It contains metal ions such as Zn, Mn, Fe etc. with molecular weight 110kDa. An aqueous epr spectrum in buffer (pH 5.6) exhibits class II mixed valence nature of Fe+3 together with Fe+2, Mn+2, Zn+2 and Cu+2 metallobiosites. It indicates reduced form of enzyme with gMn(II)= 2.0084 and grad= 2.0041 signals with radical signal. The localized electron interaction with 55Mn+2 nucleus is evidenced by six-hyperfine splitted spin allowed transitions flanked by ten satellite lines. Allowed and forbidden doublets are computed with A (55Mn) coupling constant~96 G and Zfs parameter D=0.029 cm-1. The spin integration of Tyrradical signal is shown in lyophilized sample spectrum (1.029 x 1015 spins /gm). It also shows DNA cleavage activity with pUC 19 plasmid DNA.

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