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    Two mechanisms coordinate replication termination by the Escherichia coli Tus–Ter complex

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    Type
    Article
    Authors
    Pandey, Manjula
    Elshenawy, Mohamed cc
    Jergic, Slobodan
    Takahashi, Masateru
    Dixon, Nicholas E. cc
    Hamdan, Samir cc
    Patel, Smita S.
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Date
    2015-05-24
    Online Publication Date
    2015-05-24
    Print Publication Date
    2015-07-13
    Permanent link to this record
    http://hdl.handle.net/10754/579489
    
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    Abstract
    The Escherichia coli replication terminator protein (Tus) binds to Ter sequences to block replication forks approaching from one direction. Here, we used single molecule and transient state kinetics to study responses of the heterologous phage T7 replisome to the Tus–Ter complex. The T7 replisome was arrested at the non-permissive end of Tus–Ter in a manner that is explained by a composite mousetrap and dynamic clamp model. An unpaired C(6) that forms a lock by binding into the cytosine binding pocket of Tus was most effective in arresting the replisome and mutation of C(6) removed the barrier. Isolated helicase was also blocked at the non-permissive end, but unexpectedly the isolated polymerase was not, unless C(6) was unpaired. Instead, the polymerase was blocked at the permissive end. This indicates that the Tus–Ter mechanism is sensitive to the translocation polarity of the DNA motor. The polymerase tracking along the template strand traps the C(6) to prevent lock formation; the helicase tracking along the other strand traps the complementary G(6) to aid lock formation. Our results are consistent with the model where strand separation by the helicase unpairs the GC(6) base pair and triggers lock formation immediately before the polymerase can sequester the C(6) base.
    Citation
    Two mechanisms coordinate replication termination by the Escherichia coli Tus–Ter complex 2015, 43 (12):5924 Nucleic Acids Research
    Publisher
    Oxford University Press (OUP)
    Journal
    Nucleic Acids Research
    DOI
    10.1093/nar/gkv527
    PubMed ID
    26007657
    Additional Links
    http://nar.oxfordjournals.org/lookup/doi/10.1093/nar/gkv527
    ae974a485f413a2113503eed53cd6c53
    10.1093/nar/gkv527
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program

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