Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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The DnaA Cycle in Escherichia coli: Activation, Function and Inactivation of the Initiator Protein.Low Affinity DnaA-ATP Recognition Sites in Make Non-equivalent and Growth Rate-Dependent Contributions to the Regulated Timing of Chromosome Replication

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P2860

Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli.

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

@ast

Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

@en

Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli.

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli.

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P1476

Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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P2093

Qiufen Zhang

http://www.w3.org/2001/XMLSchema#string

Shuxian Li

http://www.w3.org/2001/XMLSchema#string

Yu-Feng Yao

http://www.w3.org/2001/XMLSchema#string

Zhihong Xu

http://www.w3.org/2001/XMLSchema#string

P2860

A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin

Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration

DNA stretching by bacterial initiators promotes replication origin opening

Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation

Mechanism of origin unwinding: sequential binding of DnaA to double- and single-stranded DNA

Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica.

Polymerases and the replisome: machines within machines.

DnaA initiator--also a transcription factor.

P304

699

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P31

scholarly article

P356

10.3389/FMICB.2017.00699

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P478

http://www.w3.org/2001/XMLSchema#string

P577

2017-04-20T00:00:00Z

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P698

28473824

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P932

5397419

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Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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P2860

P2860

Acetylation of Lysine 243 Inhibits the oriC Binding Ability of DnaA in Escherichia coli

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P1433

P1476

P2093

P2860

P304

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P356

P478

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P698

P932

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P1476

P2093

P2860

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P356

P478

P577

P698

P932