Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1279-1286
Number of pages8
JournalProtein Science
Volume22
Issue number9
DOIs
Publication statusPublished - Sep 1 2013

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Escherichia coli
Biomolecular Nuclear Magnetic Resonance
Oligomerization
DNA
Chemical shift
DNA Replication
DNA Damage
Proteins
Nuclear magnetic resonance

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Medicine(all)

Cite this

Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli. / Aramaki, Takahiko; Abe, Yoshito; Katayama, Tsutomu; Ueda, Tadashi.

In: Protein Science, Vol. 22, No. 9, 01.09.2013, p. 1279-1286.

Research output: Contribution to journalArticle

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