(Q38333538)

2 September 2017

title

ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme (English)

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2 September 2017

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Hingorani MM

1

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2 September 2017

O'Donnell M

series ordinal

2

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2 September 2017

language of work or name

English

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publication date

1 September 1998

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

273

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2 September 2017

issue

38

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2 September 2017

page(s)

24550-24563

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DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine

2 September 2017

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Escherichia coli DnaX product, the tau subunit of DNA polymerase III, is a multifunctional protein with single-stranded DNA-dependent ATPase activity

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Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp

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Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp

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A separate editing exonuclease for DNA replication: the epsilon subunit of Escherichia coli DNA polymerase III holoenzyme

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Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. III. Interface between two polymerases and the clamp loader

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An explanation for lagging strand replication: polymerase hopping among DNA sliding clamps.

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Molecular matchmakers

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Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. I. Organization of the clamp loader

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Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly

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Mechanism of elongation of primed DNA by DNA polymerase delta, proliferating cell nuclear antigen, and activator 1

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DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta.delta' to a physiologically relevant range

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Cycling of Escherichia coli DNA polymerase III from one sliding clamp to another: model for lagging strand

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Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. I. Conformational changes within the gp44/62-gp45-ATP complex during clamp loading

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Protein-DNA cross-linking demonstrates stepwise ATP-dependent assembly of T4 DNA polymerase and its accessory proteins on the primer-template

21 January 2018

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DnaX complex of Escherichia coli DNA polymerase III holoenzyme. Physical characterization of the DnaX subunits and complexes

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.38.24550

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2 September 2017

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