Early Steps of Bacillus subtilis Primosome Assembly *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 276, Issue: 49, Page: 45818-45825
2001
- 70Citations
- 34Captures
- 1Mentions
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations70
- Citation Indexes70
- 70
- CrossRef68
- Captures34
- Readers34
- 34
- Mentions1
- References1
- 1
Article Description
Primosomes are nucleoprotein assemblies designed for the activation of DNA replication forks. Their primary role is to recruit the replicative helicase onto single-stranded DNA. The “replication restart” primosome, defined in Escherichia coli, is involved in the reactivation of arrested replication forks. Binding of the PriA protein to forked DNA triggers its assembly. PriA is conserved in bacteria, but its primosomal partners are not. In Bacillus subtilis, genetic analysis has revealed three primosomal proteins, DnaB, DnaD, and DnaI, that have no obvious homologues in E. coli. Interestingly, they are involved in primosome function both at arrested replication forks and at the chromosomal origin. Our biochemical analysis of the DnaB and DnaD proteins unravels their role in primosome assembly. They are both multimeric and bind individually to DNA. Furthermore, DnaD stimulates DnaB binding activities. DnaD alone and the DnaD/DnaB pair interact specifically with PriA of B. subtilis on several DNA substrates. This suggests that the nucleoprotein assembly is sequential in the PriA, DnaD, DnaB order. The preferred DNA substrate mimics an arrested DNA replication fork with unreplicated lagging strand, structurally identical to a product of recombinational repair of a stalled replication fork.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819373703; http://dx.doi.org/10.1074/jbc.m101996200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035824676&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11585815; https://linkinghub.elsevier.com/retrieve/pii/S0021925819373703; http://www.jbc.org/lookup/doi/10.1074/jbc.M101996200; https://syndication.highwire.org/content/doi/10.1074/jbc.M101996200; https://dx.doi.org/10.1074/jbc.m101996200
Elsevier BV
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