scholarly journals Role of polymeric forms of the bacteriophage phi X174 coded gene A protein in phi XRFI DNA cleavage.

1979 ◽  
Vol 254 (19) ◽  
pp. 9416-9428 ◽  
Author(s):  
J.E. Ikeda ◽  
A. Yudelevich ◽  
N. Shimamoto ◽  
J. Hurwitz
Keyword(s):  
Dna Cleavage

scholarly journals On the role of the bithiazole moiety in sequence-selective DNA cleavage by Fe.bleomycin.

1994 ◽  
Vol 269 (14) ◽  
pp. 10899-10904
Author(s):  
S.A. Kane ◽  
A. Natrajan ◽  
S.M. Hecht
Keyword(s):  
Dna Cleavage

scholarly journals TOPOVIBL-REC114 interaction regulates meiotic DNA double-strand breaks

2021 ◽  
Author(s):  
Alexandre Nore ◽  
Ariadna B Juarez-Martinez ◽  
Julie AJ Clement ◽  
Christine Brun ◽  
Bouboub Diagouraga ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Point Mutations ◽  
Double Strand Breaks ◽  
Dna Double Strand Breaks ◽  
Catalytic Complex ◽  
Strand Breaks ◽  
Genome Wide ◽  
Dna Cleavage Activity ◽  
Meiotic Dsbs

Meiosis requires the formation of programmed DNA double strand breaks (DSBs), essential for fertility and for generating genetic diversity. In male and female meiotic cells, DSBs are induced by the catalytic activity of the TOPOVIL complex formed by SPO11 and TOPOVIBL. To ensure genomic integrity, DNA cleavage activity is tightly regulated, and several accessory factors (REC114, MEI4, IHO1, and MEI1) are needed for DSB formation in mice. How and when these proteins act is not understood. Here, we show that REC114 is a direct partner of TOPOVIBL, and identified their conserved interacting domains by structural analysis. We then analysed the role of this interaction by monitoring meiotic DSBs in female and male mice carrying point mutations in TOPOVIBL that decrease or disrupt its binding to REC114. In these mutants, DSB activity was strongly reduced genome-wide in oocytes, but only in sub-telomeric regions in spermatocytes. In addition, in mutant spermatocytes, DSB activity was delayed in autosomes. These results provide evidence that REC114 is a key member of the TOPOVIL catalytic complex, and that the REC114/TOPOVIBL interaction ensures the efficiency and timing of DSB activity by integrating specific chromosomal features.

scholarly journals The Role of Mg(II) in DNA Cleavage Site Recognition in Group II Intron Ribozymes

2014 ◽  
Vol 289 (30) ◽  
pp. 20650-20663 ◽  
Author(s):  
Miriam Skilandat ◽  
Roland K. O. Sigel
Keyword(s):  
Dna Cleavage ◽  
Cleavage Site ◽  
Group Ii Intron ◽  
Group Ii ◽  
Site Recognition

scholarly journals A nucleotide resolution map of Top2-linked DNA breaks in the yeast and human genome

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
William H. Gittens ◽  
Dominic J. Johnson ◽  
Rachal M. Allison ◽  
Tim J. Cooper ◽  
Holly Thomas ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Genome Stability ◽  
Dna Double Strand Breaks ◽  
Dna Breaks ◽  
Strand Breaks ◽  
Single Strand Breaks ◽  
Human Genomes ◽  
Nucleotide Resolution

Abstract DNA topoisomerases are required to resolve DNA topological stress. Despite this essential role, abortive topoisomerase activity generates aberrant protein-linked DNA breaks, jeopardising genome stability. Here, to understand the genomic distribution and mechanisms underpinning topoisomerase-induced DNA breaks, we map Top2 DNA cleavage with strand-specific nucleotide resolution across the S. cerevisiae and human genomes—and use the meiotic Spo11 protein to validate the broad applicability of this method to explore the role of diverse topoisomerase family members. Our data characterises Mre11-dependent repair in yeast and defines two strikingly different fractions of Top2 activity in humans: tightly localised CTCF-proximal, and broadly distributed transcription-proximal, the latter correlated with gene length and expression. Moreover, single nucleotide accuracy reveals the influence primary DNA sequence has upon Top2 cleavage—distinguishing sites likely to form canonical DNA double-strand breaks (DSBs) from those predisposed to form strand-biased DNA single-strand breaks (SSBs) induced by etoposide (VP16) in vivo.

DNA cleavage by novel copper (II) complex and the role of β-cyclodextrin in promoting cleavage

2008 ◽  
Vol 16 (3) ◽  
pp. 1103-1110 ◽  
Author(s):  
Yu Huang ◽  
Qiao-Sen Lu ◽  
Ji Zhang ◽  
Zhong-Wei Zhang ◽  
Yu Zhang ◽  
...  
Keyword(s):  
Dna Cleavage

Nitric oxide-dependent pro-oxidant and pro-apoptotic effect of metallothioneins in HL-60 cells challenged with cupric nitrilotriacetate

2001 ◽  
Vol 354 (2) ◽  
pp. 397-406 ◽  
Author(s):  
Shang-Xi LIU ◽  
Kazuaki KAWAI ◽  
Vladimir A. TYURIN ◽  
Yulia Y. TYURINA ◽  
Grigory G. BORISENKO ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Caspase 3 ◽  
Protective Role ◽  
Membrane Phospholipids ◽  
No Donor ◽  
Redox Active ◽  
Apoptotic Effect ◽  
Transition And Heavy Metals ◽  
Apoptotic Effects

Intracellular safeguarding functions of metallothioneins (MTs) include sequestering transition and heavy metals, scavenging free radicals and protecting against electrophiles. We report that MT protection against Cu-induced cytotoxicity can be reversed and pro-oxidant and pro-apoptotic effects can be induced in HL-60 cells exposed to NO. We demonstrate that in ZnCl2-pretreated HL-60 cells loaded with copper nitrilotriacetate (Cu-NTA), exposure to an NO donor, S-nitroso-N-acetyl penicillamine, resulted in S-nitrosylation and oxidation of MT cysteines. This disruption of MT Cu-binding thiolate clusters caused loosening and release of redox-active Cu, enhanced redox-cycling activity of Cu and increased peroxidation of major classes of membrane phospholipids. We also found that Cu-induced oxidative stress in ZnCl2-pretreated/Cu-NTA-loaded HL-60 cells was accompanied by apoptosis documented by characteristic changes of nuclear morphology, internucleosomal DNA cleavage, externalization of phosphatidylserine, release of cytochrome c from mitochondria into cytosol and activation of caspase-3. We conclude that in Cu-challenged cells, NO can reverse the protective role of MTs and convert them into pro-oxidant, pro-apoptotic implements.

The Role of the Aminosugar and Helix Binding in the Thiol-Induced Activation of Calicheamicin for DNA Cleavage

1996 ◽  
Vol 118 (8) ◽  
pp. 1938-1948 ◽  
Author(s):  
Moneesh Chatterjee ◽  
Paul J. Smith ◽  
Craig A. Townsend
Keyword(s):  
Dna Cleavage

scholarly journals Role of factors downstream of caspases in nuclear disassembly during apoptotic execution

1999 ◽  
Vol 354 (1389) ◽  
pp. 1591-1599 ◽  
Author(s):  
K. Samejima ◽  
P. Villa ◽  
W. C. Earnshaw
Keyword(s):  
Dna Fragmentation ◽  
Dna Cleavage ◽  
Chromatin Condensation ◽  
Critical Event ◽  
Apoptotic Pathway ◽  
Independent Manner ◽  
Column Fraction ◽  
Execution Phase ◽  
Apoptotic Morphology

We used cytoplasmic extracts from chicken DU249 cells at various stages along the apoptotic pathway to analyse the events of apoptotic exe–cution. So–called S/M extracts from morphologically normal ‘committed–stage’ cells induce apoptotic morphology and DNA cleavage in substrate nuclei. These apoptotic changes appear to require the function of multiple caspases (cysteine aspar–tases, a specialized class of proteases) acting in parallel. Extracts from ‘execution–stage’ apoptotic cells induce apoptotic events in added nuclei in a caspase–independent manner. Biochemical frac–tionation of these extracts reveals that a column fraction enriched in endogenous active caspases is un–able to induce DNA fragmentation or chromatin condensation in substrate nuclei, whereas a caspase–depleted fraction induces both changes. ‘Execution–stage’ extracts contain an ICAD/DFF45–inhibitable nuclease resembling CAD, plus another activity that is required for the apoptotic chromatin condensation. ‘Committed–stage’ S/M extracts lack these downstream activities. These observations reveal that caspases act in an executive fashion, serving to activate downstream factors that disassemble the nucleus rather than disassembling it themselves. They also suggest that activation of the downstream factors (rather than the caspases) is the critical event that occurs at the transition from the latent to the execution phase of apoptosis.

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