Hda, a novel DnaA‐related protein, regulates the replication cycle in Escherichia coli
- J. Kato, T. Katayama
- BiologyEMBO Journal
- 1 August 2001
It is proposed that the once‐per‐cell‐cycle rule of replication depends on the timely interaction of AAA+ proteins that comprise the apparatus regulating the activity of the initiator of replication.
The Initiator Function of DnaA Protein Is Negatively Regulated by the Sliding Clamp of the E. coli Chromosomal Replicase
- T. Katayama, T. Kubota, K. Kurokawa, E. Crooke, K. Sekimizu
- BiologyCell
- 10 July 1998
Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC
- T. Katayama, S. Ozaki, Kenji Keyamura, K. Fujimitsu
- BiologyNature Reviews Microbiology
- 1 March 2010
The regulation of DnaA, one of the central proteins involved in bacterial DNA replication, by these factors in Escherichia coli, Bacillus subtilis and Caulobacter crescentus is described.
Specific genomic sequences of E. coli promote replicational initiation by directly reactivating ADP-DnaA.
- K. Fujimitsu, Takayuki Senriuchi, T. Katayama
- Biology, ChemistryGenes & Development
- 15 May 2009
A novel regulatory pathway is revealed that promotes the initiation of chromosomal replication via DnaA reactivation in vitro and in vivo, and which can cause synthetic lethality with a temperature-sensitive mutant dnaA and suppression of overinitiation by the lack of seqA or datA, negative regulators for initiation.
Protein Associations in DnaA-ATP Hydrolysis Mediated by the Hda-Replicase Clamp Complex*
- M. Su’etsugu, Toh-ru Shimuta, T. Ishida, H. Kawakami, T. Katayama
- BiologyJournal of Biological Chemistry
- 25 February 2005
Purified mutant Hda proteins were used in a staged in vitro RIDA system followed by a pull-down assay to show that Hda-clamp binding is a prerequisite for DnaA-ATP hydrolysis and that binding is mediated by an Hda N-terminal motif.
Cell size and nucleoid organization of engineered Escherichia coli cells with a reduced genome
- Masayuki Hashimoto, Toshiharu Ichimura, J. Kato
- BiologyMolecular Microbiology
- 25 November 2004
A simple system for formation of markerless chromosomal deletions is developed, and a series of large‐scale chromosomal deletion mutants of Escherichia coli that lack between 2.4 and 29.7% of the parental chromosome are constructed and characterized.
DiaA, a Novel DnaA-binding Protein, Ensures the Timely Initiation of Escherichia coli Chromosome Replication*
- T. Ishida, N. Akimitsu, T. Katayama
- BiologyJournal of Biological Chemistry
- 29 October 2004
It is concluded that DiaA is a novel DnaA-associating factor that is crucial to ensure the timely initiation of chromosomal replication in Escherichia coli chromosomesomal replication.
DnaA binding locus datA promotes DnaA-ATP hydrolysis to enable cell cycle-coordinated replication initiation
- Kazutoshi Kasho, T. Katayama
- BiologyProceedings of the National Academy of Sciences
- 31 December 2012
A model in which cell cycle-coordinated ATP-DnaA inactivation is regulated in a concerted manner by RIDA and datA is proposed and revealed that a complex consisting of datA and IHF promotes DnaA-ATP hydrolysis in a manner dependent on specific inter-DNAA interactions.
Formation of an ATP-DnaA-specific Initiation Complex Requires DnaA Arginine 285, a Conserved Motif in the AAA+ Protein Family*
- H. Kawakami, Kenji Keyamura, T. Katayama
- Biology, ChemistryJournal of Biological Chemistry
- 22 July 2005
It is shown that the DnaA R285A mutant is inactive for oriC replication in vivo and in vitro and that the mutation is associated with specific defects in oriC unwinding, and proposed to play a unique role in the ATP-dependent conformational activation of an initial complex.
The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes.
- Kenji Keyamura, N. Fujikawa, T. Katayama
- Biology, ChemistryGenes & Development
- 15 August 2007
The data indicate that DiaA regulates initiation by a novel mechanism, in which DiaA tetramers most likely bind to multiple DnaA molecules and stimulate the assembly of specific ATP-DnaA-oriC complexes.
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