DnaA: Controlling the Initiation of Bacterial DNA Replication and More

Kaguni, Jon M.

doi:10.1146/annurev.micro.60.080805.142111

Cited by 184 publications

(213 citation statements)

References 147 publications

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“…The DnaA AAAϩ ATPase is the initiator of replication in bacteria and functions via multiple protein-protein or protein-DNA interactions (2,3,17). Its modular architecture allows for interactions with different binding partners during the various steps of the formation of the active replication forks and coupling to other cellular events (3,15,17,20,22,29,30).…”

Section: Discussionmentioning

confidence: 99%

“…Its modular architecture allows for interactions with different binding partners during the various steps of the formation of the active replication forks and coupling to other cellular events (3,15,17,20,22,29,30). In E. coli, DnaA III interactions with itself, Hda, or DnaC are important for the spatial positioning of the ATP-DnaA molecules and their recycling (13,17,31,32).…”

Section: Discussionmentioning

confidence: 99%

“…In bacteria, the initiator protein is DnaA, a member of the AAA ϩ family of ATPases. DnaA binds to specific sequences on the origin of replication oriC, thus forming the orisome [protein-oriC complexes, reviewed in (2,3)]. Escherichia coli DnaA comprises four domains (DnaA I -DnaA IV ) (4).…”

mentioning

confidence: 99%

“…These two proteins facilitate the hydrolysis of ATP by DnaA which would lead to a disassembly of the helical arrangement and hence to the inactivation of DnaA. In E. coli, the formation of the orisome is assisted by several accessory factors such as IHF, SeqA, HU, and DiaA [reviewed in (3)], with the latter two binding directly to DnaA (15,16). The DnaA paralogue DnaC is necessary to load the DnaB helicase.…”

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confidence: 99%

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The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria

Natrajan¹,

Noirot‐Gros

Zawilak-Pawlik

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Bacterial DNA replication requires DnaA, an AAA؉ ATPase that initiates replication at a specific chromosome region, oriC, and is regulated by species-specific regulators that directly bind DnaA. HobA is a DnaA binding protein, recently identified as an essential regulator of DNA replication in Helicobacter pylori. We report the crystal structure of HobA in complex with domains I and II of DnaA (DnaA I-II ) from H. pylori, the first structure of DnaA bound to one of its regulators. Biochemical characterization of the complex formed shows that a tetramer of HobA binds four DnaA I-II molecules, and that DnaA I-II is unable to oligomerize by itself. Mutagenesis and protein-protein interaction studies demonstrate that some of the residues located at the HobA-DnaA I-II interface in the structure are necessary for complex formation. Introduction of selected mutations into H. pylori shows that the disruption of the interaction between HobA and DnaA is lethal for the bacteria. Remarkably, the DnaA binding site of HobA is conserved in DiaA from Escherichia coli, suggesting that the structure of the HobA/ DnaA complex represents a model for DnaA regulation in other Gram-negative bacteria. Our data, together with those from other studies, indicate that HobA could play a crucial scaffolding role during the initiation of replication in H. pylori by organizing the first step of DnaA oligomerization and attachment to oriC.DiaA ͉ isothermal titration calorimetry ͉ replication regulators ͉ X-ray crystallography

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria

Natrajan¹,

Noirot‐Gros

Zawilak-Pawlik

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…DnaA protein is required for the initiation of DNA replication (for review, see ref. 31), and dnaN encodes the ␤-clamp that allows for processive DNA replication (32,33). Cells bearing the dnaA::P spac dnaAN ϩ allele require IPTG for expression of dnaAN and for viability (26).…”

Section: The Subcellular Position Of Reca-gfp Foci Is Consistent Withmentioning

confidence: 99%

Replication is required for the RecA localization response to DNA damage in Bacillus subtilis

Simmons

Grossman

Walker

2007

Proc. Natl. Acad. Sci. U.S.A.

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In both prokaryotes and eukaryotes, proteins involved in DNA repair often organize into multicomponent complexes that can be visualized as foci in living cells. We used a RecA-GFP fusion to examine the subcellular cues that direct RecA-GFP to assemble as foci in response to DNA damage. We used two different methods to inhibit initiation of DNA replication and determined that DNA replication is required for the cell to establish RecA-GFP foci after exposure to DNA-damaging agents. Furthermore, use of endonuclease cleavage to generate a site-specific double-strand break demonstrated that the replication machinery (replisome) and DNA synthesis are required for assembly of RecA-GFP foci during repair of a double-strand break. We monitored the cellular levels of RecA and found that focus formation does not require further induction of protein levels, suggesting that foci result from a redistribution of existing protein to sites of damage encountered by the replisome. Taken together, our results support the model that existing RecA protein is recruited to ssDNA generated by the replisome at sites of DNA damage. These results provide insight into the mechanisms that the cell uses to recruit repair proteins to damaged DNA in living cells.replisome ͉ focus ͉ double-strand break

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Insight into initiator–DNA interactions: a lesson from the archaeal ORC

2008

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Although initiation of DNA replication is considered to be highly coordinated through multiple protein-DNA and protein-protein interactions, it is poorly understood how particular locations within the eukaryotic chromosome are selected as origins of DNA replication. Here, we discuss recent reports that present structural information on the interaction characteristics of the archaeal orthologues of the eukaryotic origin recognition complex with their cognate binding sequences. Since the archaeal replication system is postulated as a simplified version of the one in eukaryotes, by analogy, these works provide insights into the functions of the eukaryotic initiator proteins.

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DnaA: Controlling the Initiation of Bacterial DNA Replication and More

Cited by 184 publications

References 147 publications

The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria

The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria

Replication is required for the RecA localization response to DNA damage in Bacillus subtilis

Insight into initiator–DNA interactions: a lesson from the archaeal ORC

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