What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments
AuthorsBerghuis, Bojk A.
Dixon, Nicholas E.
Dekker, Nynke H.
Permanent link to this recordhttp://hdl.handle.net/10754/626136
MetadataShow full item record
AbstractSynchronizing the convergence of the two-oppositely moving DNA replication machineries at specific termination sites is a tightly coordinated process in bacteria. In 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–Ter. The exact sequence of events by which Tus–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–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–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.
CitationBerghuis 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.
SponsorsFunding for this work has been provided by the Australian Research Council (DP150100956) (to NED), by King Abdullah University of Science and Technology through core funding to (S.M.H.) and a Competitive Research Award (CRG5) (to S.M.H. and NED); and by a VICI grant from the Netherlands Organization for Scientific Research and an ERC Consolidator Grant (DynGenome, no 312221) from the European Research Council (both to N.H.D.).
PublisherInforma UK Limited
Except where otherwise noted, this item's license is described as This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
- Strand separation establishes a sustained lock at the Tus-Ter replication fork barrier.
- Authors: Berghuis BA, Dulin D, Xu ZQ, van Laar T, Cross B, Janissen R, Jergic S, Dixon NE, Depken M, Dekker NH
- Issue date: 2015 Aug
- Replisome speed determines the efficiency of the Tus-Ter replication termination barrier.
- Authors: Elshenawy MM, Jergic S, Xu ZQ, Sobhy MA, Takahashi M, Oakley AJ, Dixon NE, Hamdan SM
- Issue date: 2015 Sep 17
- Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex.
- Authors: Neylon C, Kralicek AV, Hill TM, Dixon NE
- Issue date: 2005 Sep
- Differential Tus-Ter binding and lock formation: implications for DNA replication termination in Escherichia coli.
- Authors: Moreau MJ, Schaeffer PM
- Issue date: 2012 Oct
- The progression of replication forks at natural replication barriers in live bacteria.
- Authors: Moolman MC, Tiruvadi Krishnan S, Kerssemakers JW, de Leeuw R, Lorent V, Sherratt DJ, Dekker NH
- Issue date: 2016 Jul 27