TY - JOUR
T1 - What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments
AU - Berghuis, Bojk A.
AU - Raducanu, Vlad-Stefan
AU - Elshenawy, Mohamed
AU - Jergic, Slobodan
AU - Depken, Martin
AU - Dixon, Nicholas E.
AU - Hamdan, Samir
AU - Dekker, Nynke H.
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: Funding 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.).
PY - 2017/11/6
Y1 - 2017/11/6
N2 - Synchronizing 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.
AB - Synchronizing 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.
UR - http://hdl.handle.net/10754/626136
UR - http://www.tandfonline.com/doi/full/10.1080/10409238.2017.1394264
UR - http://www.scopus.com/inward/record.url?scp=85039447823&partnerID=8YFLogxK
U2 - 10.1080/10409238.2017.1394264
DO - 10.1080/10409238.2017.1394264
M3 - Article
C2 - 29108427
VL - 53
SP - 49
EP - 63
JO - Critical Reviews in Biochemistry and Molecular Biology
JF - Critical Reviews in Biochemistry and Molecular Biology
SN - 1040-9238
IS - 1
ER -