Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement (Q38361453)

2 September 2017

title

Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement (English)

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2 September 2017

S Kim

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2 September 2017

H G Dallmann

series ordinal

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2 September 2017

C S McHenry

series ordinal

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2 September 2017

K J Marians

series ordinal

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2 September 2017

language of work or name

English

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publication date

1 February 1996

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2 September 2017

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2 September 2017

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2 September 2017

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2 September 2017

page(s)

643-650

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The replication time of the Escherichia coli K12 chromosome as a function of cell doubling time

2 September 2017

cites work

1 reference

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7 January 2021

DnaX complex of Escherichia coli DNA polymerase III holoenzyme. Central role of tau in initiation complex assembly and in determining the functional asymmetry of holoenzyme

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7 January 2021

Genetic control of mutation rates in bacteriophageT4.

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Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases

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7 January 2021

A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho

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7 January 2021

Tau protects beta in the leading-strand polymerase complex at the replication fork.

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7 January 2021

Site-specific pausing of deoxyribonucleic acid synthesis catalyzed by four forms of Escherichia coli DNA polymerase III

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7 January 2021

Prokaryotic DNA replication

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7 January 2021

Phi X174-type primosomal proteins: purification and assay

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7 January 2021

ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication

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7 January 2021

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

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https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981039-9

7 January 2021

Escherichia coli DNA polymerase III holoenzyme subunits alpha, beta, and gamma directly contact the primer-template

1 reference

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7 January 2021

Mechanism of DNA elongation catalyzed by Escherichia coli DNA polymerase III, dnaZ protein, and DNA elongation factors I and III

1 reference

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7 January 2021

Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding

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10.1016/S0092-8674(00)81039-9

Identifiers

DOI

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2 September 2017

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