Structural highlights
Function
PRIC_ECOLI PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.
Publication Abstract from PubMed
In eubacterial organisms, the oriC-independent primosome plays an essential role in replication restart after the dissociation of the replication DNA-protein complex by DNA damage. PriC is a key protein component in the replication restart primosome. Our recent study suggested that PriC is divided into two domains: an N-terminal and a C-terminal domain. In the present study, we determined the solution structure of the N-terminal domain, whose structure and function have remained unknown until now. The revealed structure was composed of three helices and one extended loop. We also observed chemical shift changes in the heteronuclear NMR spectrum and oligomerization in the presence of ssDNA. These abilities may contribute to the PriC-ssDNA complex, which is important for the replication restart primosome.
Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli.,Aramaki T, Abe Y, Katayama T, Ueda T Protein Sci. 2013 Jul 19. doi: 10.1002/pro.2314. PMID:23868391[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aramaki T, Abe Y, Katayama T, Ueda T. Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli. Protein Sci. 2013 Jul 19. doi: 10.1002/pro.2314. PMID:23868391 doi:10.1002/pro.2314
