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Full-Text Articles in Social and Behavioral Sciences
Site-Specific Covalent Attachment Of Dna To Proteins Using A Photoactivatable Tus-Ter Complex, Dahdah B. Dahdah, Isabelle Morin, Morgane Moreau, Nicholas E. Dixon, Patrick M. Schaeffer
Site-Specific Covalent Attachment Of Dna To Proteins Using A Photoactivatable Tus-Ter Complex, Dahdah B. Dahdah, Isabelle Morin, Morgane Moreau, Nicholas E. Dixon, Patrick M. Schaeffer
Professor Nick E Dixon
Investigations into the photocrosslinking kinetics of the protein Tus with various bromodeoxyuridine-substituted Ter DNA variants highlight the potential use of this complex as a photoactivatable connector between proteins of interest and specific DNA sequences.
Structure Of The Theta Subunit Of Escherichia Coli Dna Polymerase Iii In Complex With The Epsilon Subunit, Max A Keniry, Ah-Young Park, Elisabeth A. Owen, Samir M. Hamdan, Guido Pintacuda, Gottfried Otting, Nicholas E. Dixon
Structure Of The Theta Subunit Of Escherichia Coli Dna Polymerase Iii In Complex With The Epsilon Subunit, Max A Keniry, Ah-Young Park, Elisabeth A. Owen, Samir M. Hamdan, Guido Pintacuda, Gottfried Otting, Nicholas E. Dixon
Professor Nick E Dixon
The catalytic core of Escherichia coli DNA polymerase III contains three tightly associated subunits, the α, ε, and θ subunits. The θ subunit is the smallest and least understood subunit. The three-dimensional structure of θ in a complex with the unlabeled N-terminal domain of the ε subunit, ε186, was determined by multidimensional nuclear magnetic resonance spectroscopy. The structure was refined using pseudocontact shifts that resulted from inserting a lanthanide ion (Dy3+, Er3+, or Ho3+) at the active site of ε186. The structure determination revealed a three-helix bundle fold that is similar to the solution structures of θ in a methanol-water …
Replication Termination In Escherichia Coli: Structure And Anti-Helicase Activity Of The Tus-Ter Complex, Cameron Neylon, Andrew V. Kralicek, Thomas M. Hill, Nicholas E. Dixon
Replication Termination In Escherichia Coli: Structure And Anti-Helicase Activity Of The Tus-Ter Complex, Cameron Neylon, Andrew V. Kralicek, Thomas M. Hill, Nicholas E. Dixon
Professor Nick E Dixon
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 …
Proofreading Exonuclease On A Tether: The Complex Between The E. Coli Dna Polymerase Iii Subunits Α, Ε, Θ And Β Reveals A Highly Flexible Arrangement Of The Proofreading Domain, Kiyoshi Ozawa, Nicholas P. Horan, Andrew Robinson, Hiromasa Yagi, Flynn R. Hill, Slobodan Jergic, Zhi-Qiang Xu, Karin V. Loscha, Nan Li, Moeava Tehei, Aaron J. Oakley, Gottfried Otting, Thomas Huber, Nicholas E. Dixon
Proofreading Exonuclease On A Tether: The Complex Between The E. Coli Dna Polymerase Iii Subunits Α, Ε, Θ And Β Reveals A Highly Flexible Arrangement Of The Proofreading Domain, Kiyoshi Ozawa, Nicholas P. Horan, Andrew Robinson, Hiromasa Yagi, Flynn R. Hill, Slobodan Jergic, Zhi-Qiang Xu, Karin V. Loscha, Nan Li, Moeava Tehei, Aaron J. Oakley, Gottfried Otting, Thomas Huber, Nicholas E. Dixon
Professor Nick E Dixon
A complex of the three (αεθ) core subunits and the β2 sliding clamp is responsible for DNA synthesis by Pol III, the Escherichia coli chromosomal DNA replicase. The 1.7 Å crystal structure of a complex between the PHP domain of α (polymerase) and the C-terminal segment of ε (proofreading exonuclease) subunits shows that ε is attached to α at a site far from the polymerase active site. Both α and ε contain clamp-binding motifs (CBMs) that interact simultaneously with β2 in the polymerization mode of DNA replication by Pol III. Strengthening of both CBMs enables isolation of stable αεθ:β2 complexes. …