| Identification of genetic interactions with priB links the PriA/PriB DNA replication restart pathway to double-strand DNA break repair in Escherichia coli. | Identification of genetic interactions with priB links the PriA/PriB DNA replication restart pathway to double-strand DNA break repair in Escherichia coli.
McKenzie AM, Henry C, Myers KS, Place MM, Keck JL., Free PMC Article | 12/10/2022 |
| A structural model of the PriB-DnaT complex in Escherichia coli replication restart. | A structural model of the PriB-DnaT complex in Escherichia coli replication restart.
Abe Y, Ikeda Y, Fujiyama S, Kini RM, Ueda T. | 07/31/2021 |
| Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT. | Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.
Huang YH, Huang CY., Free PMC Article | 05/16/2015 |
| found that the acidic linker between the two domains had an activity for dissociating ssDNA from the PriB.ssDNA complexes in a manner supported by the conserved acidic residues Asp70 and Glu76 | Structure and mechanism of the primosome protein DnaT-functional structures for homotrimerization, dissociation of ssDNA from the PriB·ssDNA complex, and formation of the DnaT·ssDNA complex.
Fujiyama S, Abe Y, Tani J, Urabe M, Sato K, Aramaki T, Katayama T, Ueda T. | 01/31/2015 |
| A role for His64 in the compactness of the PriB-ssDNA complex and in the positive cooperativity of PriB. | Involvement of histidine in complex formation of PriB and single-stranded DNA.
Fujiyama S, Abe Y, Takenawa T, Aramaki T, Shioi S, Katayama T, Ueda T. | 04/5/2014 |
| Abolishing PriB leads to suppression of the recG null phenotype. | Modulation of DNA damage tolerance in Escherichia coli recG and ruv strains by mutations affecting PriB, the ribosome and RNA polymerase.
Mahdi AA, Briggs GS, Lloyd RG., Free PMC Article | 04/6/2013 |
| Binding mode is proposed for forming a stable complex of PriB with ssDNA of 25 nucleotides. | A single residue determines the cooperative binding property of a primosomal DNA replication protein, PriB, to single-stranded DNA.
Huang YH, Lin HH, Huang CY. | 11/17/2012 |
| PriB homolog of K. pneumoniae is similar in structure and in function to that of E. coli | The priB gene of Klebsiella pneumoniae encodes a 104-amino acid protein that is similar in structure and function to Escherichia coli PriB.
Berg L, Lopper ME., Free PMC Article | 06/9/2012 |
| 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. | Binding of two PriA-PriB complexes to the primosome assembly site initiates primosome formation.
Szymanski MR, Jezewska MJ, Bujalowski W. | 09/24/2011 |
| N-terminus verified by Edman degradation on mature peptide | See all PubMed (2) articles | 11/5/2007 |
| structure establishes a putative protein interaction surface that may contribute to the role of PriB in primosome assembly by facilitating interactions with PriA and DnaT | Crystal structure of PriB, a component of the Escherichia coli replication restart primosome.
Lopper M, Holton JM, Keck JL. | 01/21/2010 |
| crystal structure determined; crystal structure PriB is structurally identical to the N-terminal DNA-binding domain of the single-stranded DNA-binding protein (SSB);analyzed features of PriB binding to ssDNA from a view of structural comparison with SBB | Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site.
Shioi S, Ose T, Maenaka K, Shiroishi M, Abe Y, Kohda D, Katayama T, Ueda T. | 01/21/2010 |
| PriB stimulates PriA helicase, acting to increase the apparent processivity of PriA | PriB stimulates PriA helicase via an interaction with single-stranded DNA.
Cadman CJ, Lopper M, Moon PB, Keck JL, McGlynn P. | 01/21/2010 |
| This report presents the first structure of a replication restart primosomal protein complexed with DNA, and a novel model that explains the interactions between a dimeric oligonucleotide-binding-fold protein and single-stranded DNA. | Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode.
Huang CY, Hsu CH, Sun YJ, Wu HN, Hsiao CD., Free PMC Article | 01/21/2010 |
| A new dnaC mutation (dnaC824) is reported here that efficiently suppresses priB rep mutant phenotypes. | A novel dnaC mutation that suppresses priB rep mutant phenotypes in Escherichia coli K-12.
Boonsombat R, Yeh SP, Milne A, Sandler SJ. | 01/21/2010 |