Asymmetric rolling circle replication of the promiscuous replicon pMV158 is initiated by the plasmid-encoded RepB protein. In vitro, purified RepB protein introduces a nick within the leading strand origin of replication by a nucleophylic attack on the phosphodiester bond at the dinucleotide GpA. Some changes within and around this dinucleotide were recognized by the protein. RepB nicked and closed supercoiled pMV158 DNA, having an optimum activity at 60 degrees C. We have imitated, in vitro, a process of rolling circle replication, since RepB was able to nick (initiation) and to covalently close (termination) single-stranded oligonucleotides containing the protein cleavage sequence. Covalent DNA-protein complexes were not found, indicating that RepB has unique features among plasmid-encoded proteins involved in rolling-circle replication or conjugative mobilization.
The copy number of plasmid pLS1 is regulated by two trans-acting plasmid products: the antisense RNA II and the repressor protein, RepA
Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria
Specificity of origin recognition by replication initiator protein in plasmids of the pT181 family is determined by a six amino acid residue element
In vitro cleavage of double- and single-stranded DNA by plasmid RSF1010-encoded mobilization proteins
Large-scale stable opening of supercoiled DNA in response to temperature and supercoiling in (A + T)-rich regions that promote low-salt cruciform extrusion
Initiation of replication of plasmid pLS1. The initiator protein RepB acts on two distant DNA regions
Initiation of rolling-circle replication in pT181 plasmid: initiator protein enhances cruciform extrusion at the origin
Camptothecin, a specific inhibitor of type I DNA topoisomerase, induces DNA breakage at replication forks.
Replication of the streptococcal plasmid pMV158 and derivatives in cell-free extracts of Escherichia coli
Multiple DNA conformational changes induced by an initiator protein precede the nicking reaction in a rolling circle replication origin
Nopaline causes a conformational change in the NocR regulatory protein-nocR promoter complex of Agrobacterium tumefaciens Ti plasmid pTiT37
Relaxase (TraI) of IncP alpha plasmid RP4 catalyzes a site-specific cleaving-joining reaction of single-stranded DNA
DNA-binding specificity determinants of replication proteins encoded by eukaryotic ssDNA viruses are adjacent to widely separated RCR conserved motifs
Structural features of the initiator of replication protein RepB encoded by the promiscuous plasmid pMV158
Translation initiation of the replication initiator repB gene of promiscuous plasmid pMV158 is led by an extended non-SD sequence
A rolling circle replication initiator protein with a nucleotidyl-transferase activity encoded by the plasmid pGT5 from the hyperthermophilic archaeon Pyrococcus abyssi
The active site of the rolling circle replication protein Rep75 is involved in site-specific nuclease, ligase and nucleotidyl transferase activities
Catalytic domain of plasmid pAD1 relaxase TraX defines a group of relaxases related to restriction endonucleases
Why is the initiation nick site of an AT-rich rolling circle plasmid at the tip of a GC-rich cruciform?
Interactions between the RepB initiator protein of plasmid pMV158 and two distant DNA regions within the origin of replication
Specific cleavage of chromosomal and plasmid DNA strands in gram-positive and gram-negative bacteria can be detected with nucleotide resolution
Small rolling circle plasmids in Bacillus subtilis and related species: organization, distribution, and their possible role in host physiology
Plasmid replication initiator RepB forms a hexamer reminiscent of ring helicases and has mobile nuclease domains
The mobilization protein, MobM, of the streptococcal plasmid pMV158 specifically cleaves supercoiled DNA at the plasmid oriT
RepAM of the Amycolatopsis methanolica integrative element pMEA300 belongs to a novel class of replication initiator proteins
Acidic pH Decreases the Endonuclease Activity of Initiator RepB and Increases the Stability of the Covalent RepB-DNA Intermediate while Has Only a Limited Effect on the Replication of Plasmid pMV158 in Lactococcus lactis.
The two active-site tyrosine residues of the a protein play non-equivalent roles during initiation of rolling circle replication of bacteriophage p2
Initiation of replication of plasmid pMV158: mechanisms of DNA strand-transfer reactions mediated by the initiator RepB protein
In vitro recognition of the replication origin of pLS1 and of plasmids of the pLS1 family by the RepB initiator protein
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