Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family. (Q46497050)

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11 January 2020

title

Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family (English)

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11 January 2020

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11 January 2020

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11 January 2020

Kenji Keyamura

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11 January 2020

language of work or name

English

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publication date

17 May 2005

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Journal of Biological Chemistry

11 January 2020

published in

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volume

280

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issue

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page(s)

27420-27430

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

11 January 2020

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Two discriminatory binding sites in the Escherichia coli replication origin are required for DNA strand opening by initiator DnaA-ATP.

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IHF redistributes bound initiator protein, DnaA, on supercoiled oriC of Escherichia coli

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DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication.

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A nucleotide switch in the Escherichia coli DnaA protein initiates chromosomal replication: evidnece from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo

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The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation

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The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin

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Identifiers

DOI

10.1074/JBC.M502764200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15901724%20AND%20SRC:MED&resulttype=core&format=json

11 January 2020

1 reference

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