N-terminal-mediated oligomerization of DnaA drives the occupancy-dependent rejuvenation of the protein on the membrane

Aranovich, Alexander; Braier-Marcovitz, Shani; Ansbacher, Esti; Granek, Rony; Parola, Abraham H.; Fishov, Itzhak

doi:10.1042/bsr20150175

Cited by 7 publications

(11 citation statements)

References 47 publications

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“…Another possible mechanism of suppression could rely on the altered membrane properties in the metabolic mutants. The DnaA protein binds to the membrane, and the membrane phospholipids stimulate rejuvenation of DnaA-ATP [ 18 , 76 ]. Moreover, expression of genes related to the membrane synthesis was affected in the dnaA46 mutant at the restrictive temperature [ 77 ].…”

Section: Discussionmentioning

confidence: 99%

Suppression of the Escherichia coli dnaA46 mutation by changes in the activities of the pyruvate-acetate node links DNA replication regulation to central carbon metabolism

et al. 2017

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To ensure faithful transmission of genetic material to progeny cells, DNA replication is tightly regulated, mainly at the initiation step. Escherichia coli cells regulate the frequency of initiation according to growth conditions. Results of the classical, as well as the latest studies, suggest that the DNA replication in E. coli starts at a predefined, constant cell volume per chromosome but the mechanisms coordinating DNA replication with cell growth are still not fully understood. Results of recent investigations have revealed a role of metabolic pathway proteins in the control of cell division and a direct link between metabolism and DNA replication has also been suggested both in Bacillus subtilis and E. coli cells. In this work we show that defects in the acetate overflow pathway suppress the temperature-sensitivity of a defective replication initiator–DnaA under acetogenic growth conditions. Transcriptomic and metabolic analyses imply that this suppression is correlated with pyruvate accumulation, resulting from alterations in the pyruvate dehydrogenase (PDH) activity. Consequently, deletion of genes encoding the pyruvate dehydrogenase subunits likewise resulted in suppression of the thermal-sensitive growth of the dnaA46 strain. We propose that the suppressor effect may be directly related to the PDH complex activity, providing a link between an enzyme of the central carbon metabolism and DNA replication.

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Section: Discussionmentioning

confidence: 99%

Suppression of the Escherichia coli dnaA46 mutation by changes in the activities of the pyruvate-acetate node links DNA replication regulation to central carbon metabolism

et al. 2017

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“…The thickness of the arrows indicate the approximate relative contributions of the different elements to the interconversion of the different forms. Stipled arrow: the relative contribution of phospholipid mediated nucleotide exchange (Sekimizu and Kornberg, 1988 ; Aranovich et al, 2006 , 2015 ) is unknown. RIDA: Replicative inactivation of DnaA (Katayama et al, 1998 ; Kato and Katayama, 2001 ); DDAH: datA dependent ATP hydrolysis (Kasho and Katayama, 2013 ); DARS: DnaA Reactivating sequence (Fujimitsu et al, 2009 ).…”

Section: Recent Additional Features Of Regulation Of Initiation By Dnmentioning

confidence: 99%

The DnaA Tale

2018

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More than 50 years have passed since the presentation of the Replicon Model which states that a positively acting initiator interacts with a specific site on a circular chromosome molecule to initiate DNA replication. Since then, the origin of chromosome replication, oriC, has been determined as a specific region that carries sequences required for binding of positively acting initiator proteins, DnaA-boxes and DnaA proteins, respectively. In this review we will give a historical overview of significant findings which have led to the very detailed knowledge we now possess about the initiation process in bacteria using Escherichia coli as the model organism, but emphasizing that virtually all bacteria have DnaA proteins that interacts with DnaA boxes to initiate chromosome replication. We will discuss the dnaA gene regulation, the special features of the dnaA gene expression, promoter strength, and translation efficiency, as well as, the DnaA protein, its concentration, its binding to DnaA-boxes, and its binding of ATP or ADP. Furthermore, we will discuss the different models for regulation of initiation which have been proposed over the years, with particular emphasis on the Initiator Titration Model.

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“…In particular, DnaA mutated at Asn44 or lysine 54 (Lys54) located on helix α3 is insensitive to RIDA in vitro and in vivo [ 31 ]. Interestingly, E. coli domain I has also been proposed to participate in the transition of DnaA-ADP into DnaA-ATP, which is able to initiate replication [ 62 ]. Such an exchange of nucleotides, called rejuvenation, is promoted by the interaction between DnaA domain III and acidic phospholipids in the cell membrane [ 61 ].…”

Section: N-terminus Of Bacterial Dnaamentioning

confidence: 99%

“…Such an exchange of nucleotides, called rejuvenation, is promoted by the interaction between DnaA domain III and acidic phospholipids in the cell membrane [ 61 ]. However, it has recently been demonstrated that this process strongly depends on DnaA protein membrane occupancy, which affects the functional state of DnaA [ 62 , 63 ]. It was proposed that domain I is particularly important for rejuvenation associated with DnaA density-driven, cooperative oligomerization [ 62 ].…”

Section: N-terminus Of Bacterial Dnaamentioning

confidence: 99%

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The Role of the N-Terminal Domains of Bacterial Initiator DnaA in the Assembly and Regulation of the Bacterial Replication Initiation Complex

Zawilak-Pawlik

Nowaczyk

Zakrzewska‐Czerwińska

2017

Genes

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The primary role of the bacterial protein DnaA is to initiate chromosomal replication. The DnaA protein binds to DNA at the origin of chromosomal replication (oriC) and assembles into a filament that unwinds double-stranded DNA. Through interaction with various other proteins, DnaA also controls the frequency and/or timing of chromosomal replication at the initiation step. Escherichia coli DnaA also recruits DnaB helicase, which is present in unwound single-stranded DNA and in turn recruits other protein machinery for replication. Additionally, DnaA regulates the expression of certain genes in E. coli and a few other species. Acting as a multifunctional factor, DnaA is composed of four domains that have distinct, mutually dependent roles. For example, C-terminal domain IV interacts with double-stranded DnaA boxes. Domain III drives ATP-dependent oligomerization, allowing the protein to form a filament that unwinds DNA and subsequently binds to and stabilizes single-stranded DNA in the initial replication bubble; this domain also interacts with multiple proteins that control oligomerization. Domain II constitutes a flexible linker between C-terminal domains III–IV and N-terminal domain I, which mediates intermolecular interactions between DnaA and binds to other proteins that affect DnaA activity and/or formation of the initiation complex. Of these four domains, the role of the N-terminus (domains I–II) in the assembly of the initiation complex is the least understood and appears to be the most species-dependent region of the protein. Thus, in this review, we focus on the function of the N-terminus of DnaA in orisome formation and the regulation of its activity in the initiation complex in different bacteria.

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N-terminal-mediated oligomerization of DnaA drives the occupancy-dependent rejuvenation of the protein on the membrane

Cited by 7 publications

References 47 publications

Suppression of the Escherichia coli dnaA46 mutation by changes in the activities of the pyruvate-acetate node links DNA replication regulation to central carbon metabolism

Suppression of the Escherichia coli dnaA46 mutation by changes in the activities of the pyruvate-acetate node links DNA replication regulation to central carbon metabolism

The DnaA Tale

The Role of the N-Terminal Domains of Bacterial Initiator DnaA in the Assembly and Regulation of the Bacterial Replication Initiation Complex

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