Nucleic Acids Research · 2002 · 74 citations · 38 references
Life SciencesGeneticsMolecular BiologyDna ReplicationMicrobial GeneticsStructural BiologyPlasmid BiologyPlasmid GeneticsPlasmid ReplicationReplication Fork ProgressionReplication In ProkaryotesReplication TerminationAgarose Gel ElectrophoresisBacterial Dna ReplicationReplication Fork PausingReplication Fork ReversalReplication Fork StabilitySupercoilingSupercoiling DynamicsTwo-dimensional Gel Electrophoresis
To study the structure of partially replicated plasmids, we cloned the Escherichia coli polar replication terminator TerE in its active orientation at different locations in the ColE1 vector pBR18. The resulting plasmids, pBR18-TerE@StyI and pBR18-TerE@EcoRI, were analyzed by neutral/neutral two-dimensional agarose gel electrophoresis and electron microscopy. Replication forks stop at the Ter-TUS complex, leading to the accumulation of specific replication intermediates with a mass 1.26 times the mass of non-replicating plasmids for pBR18-TerE@StyI and 1.57 times for pBR18-TerE@EcoRI. The number of knotted bubbles detected after digestion with ScaI and the number and electrophoretic mobility of undigested partially replicated topoisomers reflect the changes in plasmid topology that occur in DNA molecules replicated to different extents. Exposure to increasing concentrations of chloroquine or ethidium bromide revealed that partially replicated topoisomers (CCCRIs) do not sustain positive supercoiling as efficiently as their non-replicating counterparts. It was suggested that this occurs because in partially replicated plasmids a positive DeltaLk is absorbed by regression of the replication fork. Indeed, we showed by electron microscopy that, at least in the presence of chloroquine, some of the CCCRIs of pBR18-Ter@StyI formed Holliday-like junction structures characteristic of reversed forks. However, not all the positive supercoiling was absorbed by fork reversal in the presence of high concentrations of ethidium bromide.
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The importance of repairing stalled replication forks
Michael M. Cox, Myron F. Goodman, Kenneth N. Kreuzer et al. · Nature · 2000 · 1.1K citations
RuvAB Acts at Arrested Replication Forks
Marie Seigneur, Vladimir Bidnenko, S. Dusko Ehrlich et al. · Cell · 1998 · 535 citations · Full text