dnaG Antibody

1. we propose that DnaC controls the ability of DnaB to interact with primase by modifying the conformation of the N-terminal domain of DnaB PMID: 29070678
2. Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other. PMID: 25970034
3. This study identifies the C-terminal helicase-binding domain of DnaG primase (DnaG-C) and the highly conserved C-terminal region of single-stranded DNA-binding protein as interaction sites. PMID: 23430154
4. ParB complexes P1 plasmids, ParA-ATP stimulates this interaction and ParA-ADP inhibits ParB pairing activity in a parS-independent manner. PMID: 22018490
5. the connecting helix contributes necessary structural flexibility in the primase-helicase complex at replication forks. PMID: 15649896
6. essential for IncP-9 plasmid pM3 replication PMID: 16045624
7. structural features of ParB explain how this protein can bind complex arrays of A- and B-box elements on adjacent DNA arms of the looped partition site PMID: 16306995
8. analysis of centromere pairing by a plasmid-encoded type I ParB protein PMID: 17644524
9. The structure reveals an unanticipated binding site that engages nucleic acid in two distinct configurations, indicating that it serves as a nonspecific capture and tracking locus for template DNA. PMID: 18193061
10. A single-molecule analysis of the replication kinetics with varying DnaG concentrations indicates that a cooperative binding of two or three DnaG monomers to DnaB halts synthesis by Pol III. PMID: 18223657

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KEGG: ecj:JW3038

STRING: 316385.ECDH10B_3241