Structural Synergy and Molecular Crosstalk between Bacterial Helicase Loaders and Replication Initiators (Q27652911)

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English	Structural Synergy and Molecular Crosstalk between Bacterial Helicase Loaders and Replication Initiators	scientific article

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title

Structural Synergy and Molecular Crosstalk between Bacterial Helicase Loaders and Replication Initiators (English)

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main subject

molecular crosstalk

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author

James M. Berger

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4

object named as

James M Berger

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author name string

Melissa L Mott

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1

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Jan P Erzberger

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2

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Mary M Coons

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3

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language of work or name

English

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publication date

14 November 2008

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published in

Cell

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volume

135

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issue

4

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page(s)

623-34

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cites work

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DNA replication in eukaryotic cells

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Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase

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Origin recognition and the chromosome cycle

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Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex

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Evolutionary history and higher order classification of AAA+ ATPases

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The Methanothermobacter thermautotrophicus Cdc6-2 protein, the putative helicase loader, dissociates the minichromosome maintenance helicase

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29 September 2017

DNA replication initiation: mechanisms and regulation in bacteria

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29 September 2017

Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis

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29 September 2017

DnaA: controlling the initiation of bacterial DNA replication and more

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29 September 2017

Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases.

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29 September 2017

Perpetuating the double helix: molecular machines at eukaryotic DNA replication origins

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Strand-specific loading of DnaB helicase by DnaA to a substrate mimicking unwound oriC.

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29 September 2017

The DnaC helicase loader is a dual ATP/ADP switch protein

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29 September 2017

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29 September 2017

ATPase switches controlling DNA replication initiation.

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29 September 2017

Chemistry and biology

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29 September 2017

ATP- and ADP-dnaA protein, a molecular switch in gene regulation.

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29 September 2017

Characterization of dnaC2 and dnaC28 mutants by flow cytometry

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29 September 2017

Polymerases and the replisome: machines within machines.

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29 September 2017

Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA

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29 September 2017

DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli

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29 September 2017

Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454

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29 September 2017

The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex.

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29 September 2017

The dnaA protein complex with the E. coli chromosomal replication origin (oriC) and other DNA sites.

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29 September 2017

Fine balance in the regulation of DnaB helicase by DnaC protein in replication in Escherichia coli

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29 September 2017

DnaC protein contains a modified ATP-binding motif and belongs to a novel family of ATPases including also DnaA.

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29 September 2017

Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro

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29 September 2017

Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling

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2 June 2018

Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli

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2 June 2018

Sites of dnaA protein-binding in the replication origin of the Escherichia coli K-12 chromosome

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2 June 2018

Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome

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2 June 2018

In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome.

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19 June 2018

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex

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27 November 2018

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

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27 November 2018

Essential amino acids of Escherichia coli DnaC protein in an N-terminal domain interact with DnaB helicase

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27 November 2018

The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli.

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27 November 2018

Domains of DnaA protein involved in interaction with DnaB protein, and in unwinding the Escherichia coli chromosomal origin.

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27 November 2018

AAA+ ATPases in the initiation of DNA replication

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12 December 2020

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Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin

1 reference

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PubMed

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12 December 2020

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inferred from PubMed ID database lookup

Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/19013274

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Escherichia coli mutants with temperature-sensitive synthesis of DNA

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19013274

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Escherichia coli DnaA protein. The N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19013274

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1016/J.CELL.2008.09.058

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1164267

OpenCitations bibliographic resource ID

1164267

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1164267

PMC publication ID

2610854

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1164267

PubMed publication ID

19013274

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1164267

ResearchGate publication ID

23477554

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