DnaA proteins of Escherichia coli and Bacillus subtilis: coordinate actions with single-stranded DNA-binding protein and interspecies inhibition during open complex formation at the replication origins

Krause, Margret; Messer, Walter

doi:10.1016/s0378-1119(99)00009-8

Cited by 24 publications

(36 citation statements)

References 25 publications

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“…This feature is also conserved to that in E. coli (11,41). Also, comprehensive bioinformatic analysis of eubacterial oriC sequences indicates a similar feature (Christoph Weigel, personal communications of unpublished data).…”

Section: Resultsmentioning

confidence: 62%

Highly organized DnaA– oriC complexes recruit the single-stranded DNA for replication initiation

Ozaki¹,

Katayama²

2011

Nucleic Acids Research

250

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In Escherichia coli, the replication origin oriC consists of two functional regions: the duplex unwinding element (DUE) and its flanking DnaA-assembly region (DAR). ATP-DnaA molecules multimerize on DAR, unwinding DUE for DnaB helicase loading. However, DUE-unwinding mechanisms and functional structures in DnaA–oriC complexes supporting those remain unclear. Here, using various in vitro reconstituted systems, we identify functionally distinct DnaA sub-complexes formed on DAR and reveal novel mechanisms in DUE unwinding. The DUE-flanking left-half DAR carrying high-affinity DnaA box R1 and the ATP-DnaA-preferential DnaA box R5, τ1-2 and I1-2 sites formed a DnaA sub-complex competent in DUE unwinding and ssDUE binding, thereby supporting basal DnaB loading activity. This sub-complex is further subdivided into two; the DUE-distal DnaA sub-complex formed on the ATP–DnaA-preferential sites binds ssDUE. Notably, the DUE-flanking, DnaA box R1–DnaA sub-complex recruits DUE to the DUE-distal DnaA sub-complex in concert with a DNA-bending nucleoid protein IHF, thereby promoting DUE unwinding and binding of ssDUE. The right-half DAR–DnaA sub-complex stimulated DnaB loading, consistent with in vivo analyses. Similar features are seen in DUE unwinding of the hyperthermophile, Thermotoga maritima, indicating evolutional conservation of those mechanisms.

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Section: Resultsmentioning

confidence: 62%

Highly organized DnaA– oriC complexes recruit the single-stranded DNA for replication initiation

Ozaki¹,

Katayama²

2011

Nucleic Acids Research

250

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“…Eukaryal single‐stranded DNA‐binding proteins are known to be phosphorylated on serine/threonine residues by several different kinases, and interestingly, at least one type of this phosphorylation affects the interaction of eukaryal single‐stranded DNA‐binding proteins with DNA replication origins (Szuts et al ., 2003; Vassin et al ., 2004). Bacterial single‐stranded DNA‐binding proteins also have a prominent role at the origin of DNA replication (Krause and Messer, 1999), so we were compelled to examine a possible effect of Δ ptkA mutation on DNA replication in B. subtilis . To analyse DNA replication, flow cytometry experiments were performed with slowly growing balanced cultures (Michelsen et al ., 2003), in the minimal medium with succinate as carbon source.…”

Section: Resultsmentioning

confidence: 99%

Bacillus subtilis strain deficient for the protein‐tyrosine kinase PtkA exhibits impaired DNA replication

Petranović

Michelsen

Zahradka

et al. 2007

Molecular Microbiology

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SummaryBacillus subtilis has recently come into the focus of research on bacterial protein-tyrosine phosphorylation, with several proteins kinases, phosphatases and their substrates identified in this Gram-positive model organism. B. subtilis protein-tyrosine phosphorylation system PtkA/PtpZ was previously shown to regulate the phosphorylation state of UDP-glucose dehydrogenases and single-stranded DNA-binding proteins. This promiscuity towards substrates is reminiscent of eukaryal kinases and has prompted us to investigate possible physiological effects of ptkA and ptpZ gene inactivations in this study. We were unable to identify any striking phenotypes related to control of UDP-glucose dehydrogenases, natural competence and DNA lesion repair; however, a very strong phenotype of DptkA emerged with respect to DNA replication and cell cycle control, as revealed by flow cytometry and fluorescent microscopy. B. subtilis cells lacking the kinase PtkA accumulated extra chromosome equivalents, exhibited aberrant initiation mass for DNA replication and an unusually long D period.

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“…Many bacteria contain DnaA, and their replication origins contain multiple DnaA boxes that match the E. coli DnaA box consensus (24,26). C. crescentus also requires DnaA for chromosome replication (19), but Cori lacks multiple conspicuous matches to the E. coli DnaA box consensus.…”

mentioning

confidence: 99%

A Dual Binding Site for Integration Host Factor and the Response Regulator CtrA inside the Caulobacter crescentus Replication Origin

2003

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DnaA proteins of Escherichia coli and Bacillus subtilis: coordinate actions with single-stranded DNA-binding protein and interspecies inhibition during open complex formation at the replication origins

Cited by 24 publications

References 25 publications

Highly organized DnaA– oriC complexes recruit the single-stranded DNA for replication initiation

Highly organized DnaA– oriC complexes recruit the single-stranded DNA for replication initiation

Bacillus subtilis strain deficient for the protein‐tyrosine kinase PtkA exhibits impaired DNA replication

A Dual Binding Site for Integration Host Factor and the Response Regulator CtrA inside the Caulobacter crescentus Replication Origin

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