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dc.contributor.authorBerghuis, Bojk A.
dc.contributor.authorRaducanu, Vlad-Stefan
dc.contributor.authorElshenawy, Mohamed
dc.contributor.authorJergic, Slobodan
dc.contributor.authorDepken, Martin
dc.contributor.authorDixon, Nicholas E.
dc.contributor.authorHamdan, Samir
dc.contributor.authorDekker, Nynke H.
dc.date.accessioned2020-06-29T09:55:12Z
dc.date.available2020-06-29T09:55:12Z
dc.date.issued2017
dc.identifier.citationBojk A. Berghuis, Vlad-Stefan Raducanu, Elshenawy, M. M., Jergic, S., Depken, M., Dixon, N. E., Hamdan, S. M., & Dekker, N. H. (2017). What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments. Taylor & Francis. https://doi.org/10.6084/M9.FIGSHARE.5576410.V1
dc.identifier.doi10.6084/m9.figshare.5576410.v1
dc.identifier.urihttp://hdl.handle.net/10754/663920
dc.description.abstractSynchronizing the convergence of the two-oppositely moving DNA replication machineries at specific termination sites is a tightly coordinated process in bacteria. In $\textit{Escherichia coli}$, a “replication fork trap” – found within a chromosomal region where forks are allowed to enter but not leave – is set by the protein–DNA roadblock Tus$\textit{–Ter}$. The exact sequence of events by which Tus–$\textit{Ter}$ blocks replisomes approaching from one direction but not the other has been the subject of controversy for many decades. Specific protein–protein interactions between the nonpermissive face of Tus and the approaching helicase were challenged by biochemical and structural studies. These studies show that it is the helicase-induced strand separation that triggers the formation of new Tus–$\textit{Ter}$ interactions at the nonpermissive face – interactions that result in a highly stable “locked” complex. This controversy recently gained renewed attention as three single-molecule-based studies scrutinized this elusive Tus–$\textit{Ter}$ mechanism – leading to new findings and refinement of existing models, but also generating new questions. Here, we discuss and compare the findings of each of the single-molecule studies to find their common ground, pinpoint the crucial differences that remain, and push the understanding of this bipartite DNA–protein system further.
dc.publisherfigshare
dc.subjectBiophysics
dc.subjectBiochemistry
dc.subjectMicrobiology
dc.subjectCell Biology
dc.subjectMolecular Biology
dc.subjectEvolutionary Biology
dc.subjectCancer
dc.subject111714 Mental Health
dc.subject110309 Infectious Diseases
dc.titleWhat is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments
dc.typeDataset
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentChemical Engineering Program
dc.contributor.departmentLaboratory of DNA Replication and Recombination
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.contributor.institutionDepartment of Bionanoscience, Kavli institute of Nanoscience, Delft University of Technology, Delft, the Netherlands;
dc.contributor.institutionCentre for Medical and Molecular Bioscience, University of Wollongong, Wollongong, New South Wales, Australia
kaust.personRaducanu, Vlad-Stefan
kaust.personElshenawy, Mohamed
kaust.personHamdan, Samir
dc.relation.issupplementtoDOI:10.1080/10409238.2017.1394264
display.relations<b> Is Supplement To:</b><br/> <ul> <li><i>[Article]</i> <br/> Berghuis BA, Raducanu V-S, Elshenawy MM, Jergic S, Depken M, et al. (2017) What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments. Critical Reviews in Biochemistry and Molecular Biology: 1–15. Available: http://dx.doi.org/10.1080/10409238.2017.1394264.. DOI: <a href="https://doi.org/10.1080/10409238.2017.1394264" >10.1080/10409238.2017.1394264</a> HANDLE: <a href="http://hdl.handle.net/10754/626136">10754/626136</a></li></ul>


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