priA Antibody

1. observations lead to a model in which coordinated parental-, leading-, and lagging-strand DNA binding provide PriA with the structural specificity needed to act on abandoned DNA replication forks. PMID: 30201718
2. Both the N-terminal and the C-terminal fragments of PriA are required for activity, and the N-terminal fragment can be optimized to yield wild-type activity. PMID: 28607160
3. We speculate that replication pausing and fork-slow-down shortly after initiation may represent a novel checkpoint that ensures the presence of sufficient nucleotide supply prior to commitment to duplication of the entire genome. PMID: 26801562
4. Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT. PMID: 25136561
5. A small number of interacting nucleotides indicates that the DNA-binding subsites of the PriA helicase, i.e., the strong subsite on the helicase domain and the weak subsite on the N-terminal domain, are spatially separated in the intact enzyme. PMID: 21888358
6. Binding of the PriB dimer to the PriA- primosome assembly site complex dramatically increases PriA's affinity for the strong site, but only slightly affects its affinity for the weak site. PMID: 21641914
7. The strong DNA-binding subsite of the enzyme is located on the helicase domain of the PriA protein. PMID: 20624397
8. Escherichia coli PriA helicase specifically recognizes gapped DNA substrates PMID: 20089865
9. PriA-catalysed unwinding of branched DNA substrates is stimulated specifically by contact with the single-strand DNA binding protein of E.coli, SSB. PMID: 15576682
10. PriB stimulates PriA helicase, acting to increase the apparent processivity of PriA PMID: 16188886
11. crystallized an N-terminal fragment of PriA in the absence and the presence of oligonucleotides to elucidate the structural basis for the specific recognition of the 3' terminus of DNA PMID: 16226927

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KEGG: ecj:JW3906

STRING: 316385.ECDH10B_4124