Protein – Protein Interactions in the Eubacterial Replisome

Schaeffer, Patrick M.; Headlam, Madeleine J.; Dixon, Nicholas E.

doi:10.1080/15216540500058956

Cited by 75 publications

(85 citation statements)

References 72 publications

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“…The roles of the individual protein components of the replisome and the macromolecular interactions that determine its structure and function have been the subject of intensive study over the past 25 years, and this has led to sophisticated models for how the complex works. These have been the subject of recent reviews (8,15,34,35,118,153).…”

Section: Scopementioning

confidence: 99%

“…Several aspects of replication termination (7,13,19,26,58,67,78,108,120,145,153) and Tus-Ter interaction (85,170) have been reviewed previously. Although discussion here is limited to the system as it has evolved in E. coli and closely related eubacteria, understanding of termination in E. coli has developed in parallel with work on the mechanistically related system in Bacillus subtilis (26,169).…”

Section: Scopementioning

confidence: 99%

See 1 more Smart Citation

Replication Termination inEscherichia coli: Structure and Antihelicase Activity of the Tus-TerComplex

Neylon

Kralicek

Hill

et al. 2005

Microbiol Mol Biol Rev

134

144

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The arrest of DNA replication in Escherichia coli is triggered by the encounter of a replisome with a Tus protein-Ter DNA complex. A replication fork can pass through a Tus-Ter complex when traveling in one direction but not the other, and the chromosomal Ter sites are oriented so replication forks can enter, but not exit, the terminus region. The Tus-Ter complex acts by blocking the action of the replicative DnaB helicase, but details of the mechanism are uncertain. One proposed mechanism involves a specific interaction between Tus-Ter and the helicase that prevents further DNA unwinding, while another is that the Tus-Ter complex itself is sufficient to block the helicase in a polar manner, without the need for specific protein-protein interactions. This review integrates three decades of experimental information on the action of the Tus-Ter complex with information available from the Tus-TerA crystal structure. We conclude that while it is possible to explain polar fork arrest by a mechanism involving only the Tus-Ter interaction, there are also strong indications of a role for specific Tus-DnaB interactions. The evidence suggests, therefore, that the termination system is more subtle and complex than may have been assumed. We describe some further experiments and insights that may assist in unraveling the details of this fascinating process

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Section: Scopementioning

confidence: 99%

Section: Scopementioning

confidence: 99%

Replication Termination inEscherichia coli: Structure and Antihelicase Activity of the Tus-TerComplex

Neylon

Kralicek

Hill

et al. 2005

Microbiol Mol Biol Rev

134

144

View full text Add to dashboard Cite

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“…The hexameric SF4 helicase DnaB from E. coli unwinds dsDNA ahead of the replication fork thereby providing ssDNA templates for the DNA polymerase II holoenzyme (78). The results of recent single-molecule experiments indicate a macroscopic rate of (390 ± 15) nt/s for the translocation of DnaB along ssDNA (79).…”

Section: Sf3 Through Sf6 Family Helicasesmentioning

confidence: 85%

All motors have to decide is what to do with the DNA that is given them

Briggs

Fischer

2014

Biomolecular Concepts

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DNA translocases are a diverse group of molecular motors responsible for a wide variety of cellular functions. The goal of this review is to identify common aspects in the mechanisms for how these enzymes couple the binding and hydrolysis of ATP to their movement along DNA. Not surprisingly, the shared structural components contained within the catalytic domains of several of these motors appear to give rise to common aspects of DNA translocation. Perhaps more interesting, however, are the differences between the families of translocases and the potential associated implications both for the functions of the members of these families and for the evolution of these families. However, as there are few translocases for which complete characterizations of the mechanisms of DNA binding, DNA translocation, and DNA-stimulated ATPase have been completed, it is difficult to form many inferences. We therefore hope that this review motivates the necessary further experimentation required for broader comparisons and conclusions.

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“…The -subunit is that which really has the activity of DNA polymerase whereas the small subunit has proofreading 3'-5' exonuclease activity and its function is to remove nucleotides that have been misincorporated by the corepolymerase. The -subunit is stabilized by the θ-subunit, which as yet has not been assigned additional functions (Schaeffer et al, 2005). The clamp-loader or DnaX complex consists of six different subunits ( ', , , τ, , ).…”

Section: Elongation Of Dnamentioning

confidence: 99%