Two forms of ribosomal protein L2 of Escherichia coli that inhibit DnaA in DNA replication

Chodavarapu, Sundari; Felczak, Magdalena M.; Kaguni, Jon M.

doi:10.1093/nar/gkq1203

Cited by 32 publications

(38 citation statements)

References 67 publications

(91 reference statements)

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“…DiaA and its homologs appear to function by forming homotetramers that bind to the N terminus of DnaA (259,260), facilitating cooperative interactions between initiator protomers to maintain replication synchrony (260). Other proteins also bind to the N-terminal domain of E. coli DnaA; however, some of these interactions (such as the L2 ribosomal subunit) interfere with DnaA assembly to negatively regulate initiator activity (261). For its part, B. subtilis utilizes a different set of factors that binds to and controls DnaA, in particular SirA and Soj, which govern how the initiator associates with both itself and oriC (70,(262)(263)(264).…”

Section: Control Of Dnaa Functionmentioning

confidence: 99%

Mechanisms for initiating cellular DNA replication

Bleichert

Botchan

Berger

2017

Science

196

172

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The initiation of DNA replication represents a committing step to cell proliferation. Appropriate replication onset depends on multiprotein complexes that help properly distinguish origin regions, generate nascent replication bubbles, and promote replisome formation. This review describes initiation systems employed by bacteria, archaea, and eukaryotes, with a focus on comparing and contrasting molecular mechanisms among organisms. Although commonalities can be found in the functional domains and strategies used to carry out and regulate initiation, many key participants have markedly different activities and appear to have evolved convergently. Despite significant advances in the field, major questions still persist in understanding how initiation programs are executed at the molecular level.

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Section: Control Of Dnaa Functionmentioning

confidence: 99%

Mechanisms for initiating cellular DNA replication

Bleichert

Botchan

Berger

2017

Science

196

172

View full text Add to dashboard Cite

show abstract

“…DiaA and its homologs appear to function by forming homotetramers that bind to the N terminus of DnaA (259, 260), facilitating cooperative interactions between initiator protomers to maintain replication synchrony (260). Other proteins also bind to the N-terminal domain of E. coli DnaA; however, some of these interactions (such as the L2 ribosomal subunit) interfere with DnaA assembly to negatively regulate initiator activity (261). For its part, B. subtilis utilizes a different set of factors that binds to and controls DnaA, in particular SirA and Soj, which govern how the initiator associates with both itself and oriC (70, 262-264).…”

Section: Regulation Of Initiation Factorsmentioning

confidence: 99%

Mechanisms for Initiating Cellular DNA Replication

Costa

Hood

Berger

2013

Annu. Rev. Biochem.

168

169

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“…Domain I of E. coli DnaA also interacts with Dps [93], ribosomal protein L2 [94], and Hda [95]. Dps is a stress-induced protein that protects the bacterial chromosome from DNA damage by sequestering and oxidizing Fe 2+ [96,97] (reviewed in Refs.…”

Section: Mechanism Of Initiationmentioning

confidence: 99%

Replication Initiation in Bacteria

Chodavarapu

Kaguni

2016

The Enzymes

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The initiation of chromosomal DNA replication starts at a replication origin, which in bacteria is a discrete locus that contains DNA sequence motifs recognized by an initiator protein whose role is to assemble the replication fork machinery at this site. In bacteria with a single chromosome, DnaA is the initiator and is highly conserved in all bacteria. As an adenine nucleotide binding protein, DnaA bound to ATP is active in the assembly of a DnaA oligomer onto these sites. Other proteins modulate DnaA oligomerization via their interaction with the N-terminal region of DnaA. Following the DnaA-dependent unwinding of an AT-rich region within the replication origin, DnaA then mediates the binding of DnaB, the replicative DNA helicase, in a complex with DnaC to form an intermediate named the prepriming complex. In the formation of this intermediate, the helicase is loaded onto the unwound region within the replication origin. As DnaC bound to DnaB inhibits its activity as a DNA helicase, DnaC must dissociate to activate DnaB. Apparently, the interaction of DnaB with primase (DnaG) and primer formation leads to the release of DnaC from DnaB, which is coordinated with or followed by translocation of DnaB to the junction of the replication fork. There, DnaB is able to coordinate its activity as a DNA helicase with the cellular replicase, DNA polymerase III holoenzyme, which uses the primers made by primase for leading strand DNA synthesis.

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Two forms of ribosomal protein L2 of Escherichia coli that inhibit DnaA in DNA replication

Cited by 32 publications

References 67 publications

Mechanisms for initiating cellular DNA replication

Mechanisms for initiating cellular DNA replication

Mechanisms for Initiating Cellular DNA Replication

Replication Initiation in Bacteria

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