Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli

Takahiko Aramaki, Yoshito Abe, Takatoshi Ohkuri, Tomonori Mishima, Shoji Yamashita, Tsutomu Katayama, Tadashi Ueda

研究成果: ジャーナルへの寄稿記事

6 引用 (Scopus)

抄録

In Escherichia coli the oriC-independent primosome plays an essential role in replication restart after dissociation of the replication DNA-protein complex by DNA damage. Primosome is thought to form via two pathways: one PriA dependent and the other PriA independent. PriC is a key protein in the replication restart of the PriA-independent pathway. In this study, we determined that PriC was divided into two domains. Then, we obtained information that: (i) the C-terminal domain preferentially binds to single-stranded DNA (ssDNA); (ii) the binding of PriC to ssDNA depends on salt concentration; and (iii) the binding site size of PriC is approximately 7-9 nucleotides. The protease digestion of PriC suggested that a possible DNA-binding site is the N-terminus of the C-terminal domain where basic amino acid residues are concentrated. Interestingly, α-helical induction of the C-terminal domain of PriC occurred after the addition of DNAs. Also, we examined the role of heptad repeat of leucine or valine residues in the C-terminal domain and PriC oligomerization. This study describes the structure and function analysis of PriC which forms the primosome complex in replication restart.

元の言語英語
ページ(範囲)723-732
ページ数10
ジャーナルGenes to Cells
18
発行部数9
DOI
出版物ステータス出版済み - 9 1 2013

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Single-Stranded DNA
Binding Sites
Escherichia coli
Basic Amino Acids
DNA
Valine
DNA Replication
Leucine
DNA Damage
Digestion
Proteins
Peptide Hydrolases
Nucleotides
Salts

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

これを引用

Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli. / Aramaki, Takahiko; Abe, Yoshito; Ohkuri, Takatoshi; Mishima, Tomonori; Yamashita, Shoji; Katayama, Tsutomu; Ueda, Tadashi.

:: Genes to Cells, 巻 18, 番号 9, 01.09.2013, p. 723-732.

研究成果: ジャーナルへの寄稿記事

Aramaki, Takahiko ; Abe, Yoshito ; Ohkuri, Takatoshi ; Mishima, Tomonori ; Yamashita, Shoji ; Katayama, Tsutomu ; Ueda, Tadashi. / Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli. :: Genes to Cells. 2013 ; 巻 18, 番号 9. pp. 723-732.
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abstract = "In Escherichia coli the oriC-independent primosome plays an essential role in replication restart after dissociation of the replication DNA-protein complex by DNA damage. Primosome is thought to form via two pathways: one PriA dependent and the other PriA independent. PriC is a key protein in the replication restart of the PriA-independent pathway. In this study, we determined that PriC was divided into two domains. Then, we obtained information that: (i) the C-terminal domain preferentially binds to single-stranded DNA (ssDNA); (ii) the binding of PriC to ssDNA depends on salt concentration; and (iii) the binding site size of PriC is approximately 7-9 nucleotides. The protease digestion of PriC suggested that a possible DNA-binding site is the N-terminus of the C-terminal domain where basic amino acid residues are concentrated. Interestingly, α-helical induction of the C-terminal domain of PriC occurred after the addition of DNAs. Also, we examined the role of heptad repeat of leucine or valine residues in the C-terminal domain and PriC oligomerization. This study describes the structure and function analysis of PriC which forms the primosome complex in replication restart.",
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AU - Aramaki, Takahiko

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AU - Ohkuri, Takatoshi

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AU - Yamashita, Shoji

AU - Katayama, Tsutomu

AU - Ueda, Tadashi

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N2 - In Escherichia coli the oriC-independent primosome plays an essential role in replication restart after dissociation of the replication DNA-protein complex by DNA damage. Primosome is thought to form via two pathways: one PriA dependent and the other PriA independent. PriC is a key protein in the replication restart of the PriA-independent pathway. In this study, we determined that PriC was divided into two domains. Then, we obtained information that: (i) the C-terminal domain preferentially binds to single-stranded DNA (ssDNA); (ii) the binding of PriC to ssDNA depends on salt concentration; and (iii) the binding site size of PriC is approximately 7-9 nucleotides. The protease digestion of PriC suggested that a possible DNA-binding site is the N-terminus of the C-terminal domain where basic amino acid residues are concentrated. Interestingly, α-helical induction of the C-terminal domain of PriC occurred after the addition of DNAs. Also, we examined the role of heptad repeat of leucine or valine residues in the C-terminal domain and PriC oligomerization. This study describes the structure and function analysis of PriC which forms the primosome complex in replication restart.

AB - In Escherichia coli the oriC-independent primosome plays an essential role in replication restart after dissociation of the replication DNA-protein complex by DNA damage. Primosome is thought to form via two pathways: one PriA dependent and the other PriA independent. PriC is a key protein in the replication restart of the PriA-independent pathway. In this study, we determined that PriC was divided into two domains. Then, we obtained information that: (i) the C-terminal domain preferentially binds to single-stranded DNA (ssDNA); (ii) the binding of PriC to ssDNA depends on salt concentration; and (iii) the binding site size of PriC is approximately 7-9 nucleotides. The protease digestion of PriC suggested that a possible DNA-binding site is the N-terminus of the C-terminal domain where basic amino acid residues are concentrated. Interestingly, α-helical induction of the C-terminal domain of PriC occurred after the addition of DNAs. Also, we examined the role of heptad repeat of leucine or valine residues in the C-terminal domain and PriC oligomerization. This study describes the structure and function analysis of PriC which forms the primosome complex in replication restart.

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