title: Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli.
abstract: 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.
authors.affiliation: Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, 812-8582, Japan.
authors.forename: Takahiko
authors.initials: T
authors.lastname: Aramaki
authors.forename: Yoshito
authors.initials: Y
authors.lastname: Abe
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Katayama
authors.forename: Tadashi
authors.initials: T
authors.lastname: Ueda
mesh_terms: D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012996:Solutions
chemical_list: D004277:DNA, Single-Stranded; D029968:Escherichia coli Proteins; D012996:Solutions; C069995:PriC protein, E coli
keywords: NMR; PriC; primosome; protein structure; protein-DNA interaction; replication restart