Two mechanisms coordinate replication termination by the Escherichia coli Tus–Ter complex
Type
ArticleAuthors
Pandey, ManjulaElshenawy, Mohamed

Jergic, Slobodan
Takahashi, Masateru
Dixon, Nicholas E.

Hamdan, Samir

Patel, Smita S.
KAUST Department
Biological and Environmental Sciences and Engineering (BESE) DivisionBioscience Program
Date
2015-05-24Online Publication Date
2015-05-24Print Publication Date
2015-07-13Permanent link to this record
http://hdl.handle.net/10754/579489
Metadata
Show full item recordAbstract
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 ResearchPublisher
Oxford University Press (OUP)Journal
Nucleic Acids ResearchPubMed ID
26007657Additional Links
http://nar.oxfordjournals.org/lookup/doi/10.1093/nar/gkv527ae974a485f413a2113503eed53cd6c53
10.1093/nar/gkv527
Scopus Count
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