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| [[Image:2pnh.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2pnh| PDB=2pnh | SCENE= }} | | {{STRUCTURE_2pnh| PDB=2pnh | SCENE= }} |
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| '''Escherichia coli PriB E39A variant'''
| | ===Escherichia coli PriB E39A variant=== |
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| ==Overview==
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| Collapsed DNA replication forks must be reactivated through origin-independent reloading of the replication machinery (replisome) to ensure complete duplication of cellular genomes. In E. coli, the PriA-dependent pathway is the major replication restart mechanism and requires primosome proteins PriA, PriB, and DnaT for replisome reloading. However, the molecular mechanisms that regulate origin-independent replisome loading are not fully understood. Here, we demonstrate that assembly of primosome protein complexes represents a key regulatory mechanism, as inherently weak PriA-PriB and PriB-DnaT interactions are strongly stimulated by single-stranded DNA. Furthermore, the binding site on PriB for single-stranded DNA partially overlaps the binding sites for PriA and DnaT, suggesting a dynamic primosome assembly process in which single-stranded DNA is handed off from one primosome protein to another as a repaired replication fork is reactivated. This model helps explain how origin-independent initiation of DNA replication is restricted to repaired replication forks, preventing overreplication of the genome.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17588514}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17588514 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17588514}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Dna binding protein]] | | [[Category: Dna binding protein]] |
| [[Category: Ob fold]] | | [[Category: Ob fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:28:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:33:11 2008'' |