scholarly journals LET Dependence of DNA Single-Strand Scission in E. coli Bs-1 by Charged Particles

1974 ◽  
Vol 15 (3) ◽  
pp. 148-155
Author(s):  
K. IGARASHI ◽  
F. YATAGAI ◽  
T. TAKAHASHI ◽  
A. MATSUYAMA
Keyword(s):  
Charged Particles ◽  
Single Strand ◽  
Strand Scission ◽  
E Coli

scholarly journals Sinorhizobium meliloti YbeY is a zinc-dependent single-strand specific endoribonuclease that plays an important role in 16S ribosomal RNA processing

2019 ◽  
Vol 48 (1) ◽  
pp. 332-348 ◽  
Author(s):  
Vignesh M P Babu ◽  
Siva Sankari ◽  
James A Budnick ◽  
Clayton C Caswell ◽  
Graham C Walker
Keyword(s):  
16S Rrna ◽  
Metal Ion ◽  
Sinorhizobium Meliloti ◽  
Single Strand ◽  
Rrna Processing ◽  
E Coli ◽  
Gamma Proteobacteria ◽  
Ribosomal Rna Processing ◽  
Alpha Proteobacteria ◽  
Endoribonuclease Activity

Abstract Single-strand specific endoribonuclease YbeY has been shown to play an important role in the processing of the 3′ end of the 16S rRNA in Escherichia coli. Lack of YbeY results in the accumulation of the 17S rRNA precursor. In contrast to a previous report, we show that Sinorhizobium meliloti YbeY exhibits endoribonuclease activity on single-stranded RNA substrate but not on the double-stranded substrate. This study also identifies the previously unknown metal ion involved in YbeY function to be Zn2+ and shows that the activity of YbeY is enhanced when the occupancy of zinc is increased. We have identified a pre-16S rRNA precursor that accumulates in the S. meliloti ΔybeY strain. We also show that ΔybeY mutant of Brucella abortus, a mammalian pathogen, also accumulates a similar pre-16S rRNA. The pre-16S species is longer in alpha-proteobacteria than in gamma-proteobacteria. We demonstrate that the YbeY from E. coli and S. meliloti can reciprocally complement the rRNA processing defect in a ΔybeY mutant of the other organism. These results establish YbeY as a zinc-dependent single-strand specific endoribonuclease that functions in 16S rRNA processing in both alpha- and gamma-proteobacteria.

scholarly journals Specific cleavage of the terminal protein from the adenovirus 5 DNA under the condition of single-strand scission by nuclease S1

FEBS Letters ◽  
1979 ◽  
Vol 107 (2) ◽  
pp. 355-358 ◽  
Author(s):  
Hiroyoshi Ariga ◽  
Hiroto Shimojo ◽  
So Hidaka ◽  
Kin-ichiro Miura
Keyword(s):  
Single Strand ◽  
Terminal Protein ◽  
Strand Scission ◽  
Nuclease S1 ◽  
Adenovirus 5

scholarly journals Induction of a DNA Nickase in the Presence of Its Target Site Stimulates Adaptive Mutation in Escherichia coli

2002 ◽  
Vol 184 (20) ◽  
pp. 5599-5608 ◽  
Author(s):  
Cesar Rodriguez ◽  
Joshua Tompkin ◽  
Jill Hazel ◽  
Patricia L. Foster
Keyword(s):  
Escherichia Coli ◽  
Single Strand ◽  
Target Site ◽  
Adaptive Mutation ◽  
Target Sequence ◽  
Induced Mutations ◽  
Single Base ◽  
Adaptive Mutations ◽  
E Coli ◽  
Nicking Enzyme

ABSTRACT Adaptive mutation to Lac+ in Escherichia coli strain FC40 depends on recombination functions and is enhanced by the expression of conjugal functions. To test the hypothesis that the conjugal function that is important for adaptive mutation is the production of a single-strand nick at the conjugal origin, we supplied an exogenous nicking enzyme, the gene II protein (gIIp) of bacteriophage f1, and placed its target sequence near the lac allele. When both gIIp and its target site were present, adaptive mutation was stimulated three- to fourfold. Like normal adaptive mutations, gIIp-induced mutations were recA+ and ruvC+ dependent and were mainly single-base deletions in runs of iterated bases. In addition, gIIp with its target site could substitute for conjugal functions in adaptive mutation. These results support the hypothesis that nicking at the conjugal origin initiates the recombination that produces adaptive mutations in this strain of E. coli, and they suggest that nicking may be the only conjugal function required for adaptive mutation.

Studies related to antitumor antibiotics. Part VII. Synthesis of streptonigrin analogues and their single strand scission of DNA

1976 ◽  
Vol 54 (16) ◽  
pp. 2563-2572 ◽  
Author(s):  
J. William Lown ◽  
Soo-Khoon Sim
Keyword(s):  
Antitumor Activity ◽  
Dna Cleavage ◽  
Single Strand ◽  
Antitumor Antibiotic ◽  
Antitumor Antibiotics ◽  
Substitution Pattern ◽  
Circular Dna ◽  
Strand Scission ◽  
Independent Synthesis ◽  
Selective Catalysis

The syntheses of a group of 2-(o-nitrophenyl)- and 2-(o-aminophenyl)-5,8-quinolinediones which are structurally related to the antitumor antibiotic streptonigrin are described. Ambiguities in the position of required nucleophilic displacements are resolved by independent synthesis. The rates of single strand cleavage of PM2 ccc-DNA (covalently-closed circular-DNA) induced by these compounds are compared, which correlates with antitumor activity. The 2-(o-nitrophenyl) derivatives give consistently more rapid DNA cleavage than the 2-(o-aminophenyl) compounds. The autoxidations of the dihydroxyquinolines are subject to selective catalysis by Cu2+ on. 2-(o-Aminophenyl)-7-amino-6-methoxy-5,6-quinolinedione which has a substitution pattern most closely resembling streptonigrin also closely parallels the rate of scission of DNA of the latter in the presence of NADPH.

Covalent modification and single-strand scission of DNA by a new antitumor antibiotic kapurimycin A3

Biochemistry ◽  
1990 ◽  
Vol 29 (46) ◽  
pp. 10449-10455 ◽  
Author(s):  
Mitsunobu Hara ◽  
Mayumi Yoshida ◽  
Hirofumi Nakano
Keyword(s):  
Covalent Modification ◽  
Single Strand ◽  
Antitumor Antibiotic ◽  
Strand Scission

scholarly journals Plasmid replication-associated single-strand-specific methyltransferases

2020 ◽  
Vol 48 (22) ◽  
pp. 12858-12873
Author(s):  
Alexey Fomenkov ◽  
Zhiyi Sun ◽  
Iain A Murray ◽  
Cristian Ruse ◽  
Colleen McClung ◽  
...  
Keyword(s):  
Restriction Enzymes ◽  
Dna Methyltransferases ◽  
Single Strand ◽  
Burkholderia Cenocepacia ◽  
Dna Polymerase I ◽  
E Coli ◽  
New Hosts ◽  
Dna Strand ◽  
Polymerase I

Abstract Analysis of genomic DNA from pathogenic strains of Burkholderia cenocepacia J2315 and Escherichia coli O104:H4 revealed the presence of two unusual MTase genes. Both are plasmid-borne ORFs, carried by pBCA072 for B. cenocepacia J2315 and pESBL for E. coli O104:H4. Pacific Biosciences SMRT sequencing was used to investigate DNA methyltransferases M.BceJIII and M.EcoGIX, using artificial constructs. Mating properties of engineered pESBL derivatives were also investigated. Both MTases yield promiscuous m6A modification of single strands, in the context SAY (where S = C or G and Y = C or T). Strikingly, this methylation is asymmetric in vivo, detected almost exclusively on one DNA strand, and is incomplete: typically, around 40% of susceptible motifs are modified. Genetic and biochemical studies suggest that enzyme action depends on replication mode: DNA Polymerase I (PolI)-dependent ColE1 and p15A origins support asymmetric modification, while the PolI-independent pSC101 origin does not. An MTase-PolI complex may enable discrimination of PolI-dependent and independent plasmid origins. M.EcoGIX helps to establish pESBL in new hosts by blocking the action of restriction enzymes, in an orientation-dependent fashion. Expression and action appear to occur on the entering single strand in the recipient, early in conjugal transfer, until lagging-strand replication creates the double-stranded form.

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