Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA

Kaori Tabata, Toyoyuki Ose, Naoaki Okamoto, Katsumi Maenaka, Taku Tanaka, Hisao Masai, Mihoko Saito, Tsuyoshi Shirai, Daisuke Kohda

研究成果: ジャーナルへの寄稿記事

33 引用 (Scopus)

抄録

In eubacteria, PriA helicase detects the stalled DNA replication forks. This critical role of PriA is ascribed to its ability to bind to the 3′ end of a nascent leading DNA strand in the stalled replication forks. The crystal structures in complexes with oligonucleotides and the combination of fluorescence correlation spectroscopy and mutagenesis reveal that the N-terminal domain of PriA possesses a binding pocket for the 3′-terminal nucleotide residue of DNA. The interaction with the deoxyribose 3′-OH is essential for the 3′-terminal recognition. In contrast, the direct interaction with 3′-end nucleobase is unexpected, considering the same affinity for oligonucleotides carrying the four bases at the 3′ end. Thus, the N-terminal domain of PriA recognizes the 3′-end base in a base-non-selective manner, in addition to the deoxyribose and 5′-side phosphodiester group, of the 3′-terminal nucleotide to acquire both sufficient affinity and non-selectivity to find all of the stalled replication forks generated during DNA duplication. This unique feature is prerequisite for the proper positioning of the helicase domain of PriA on the unreplicated double-stranded DNA.

元の言語英語
ページ(範囲)2584-2593
ページ数10
ジャーナルEMBO Journal
26
発行部数10
DOI
出版物ステータス出版済み - 5 16 2007

Fingerprint

DNA
Oligonucleotides
Nucleotides
Deoxyribose
Fluorescence Spectrometry
DNA Replication
Mutagenesis
Bacteria
Crystal structure
Fluorescence
Spectroscopy
3-deoxyribose

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

これを引用

Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA. / Tabata, Kaori; Ose, Toyoyuki; Okamoto, Naoaki; Maenaka, Katsumi; Tanaka, Taku; Masai, Hisao; Saito, Mihoko; Shirai, Tsuyoshi; Kohda, Daisuke.

:: EMBO Journal, 巻 26, 番号 10, 16.05.2007, p. 2584-2593.

研究成果: ジャーナルへの寄稿記事

Tabata, K, Ose, T, Okamoto, N, Maenaka, K, Tanaka, T, Masai, H, Saito, M, Shirai, T & Kohda, D 2007, 'Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA', EMBO Journal, 巻. 26, 番号 10, pp. 2584-2593. https://doi.org/10.1038/sj.emboj.7601697
Tabata, Kaori ; Ose, Toyoyuki ; Okamoto, Naoaki ; Maenaka, Katsumi ; Tanaka, Taku ; Masai, Hisao ; Saito, Mihoko ; Shirai, Tsuyoshi ; Kohda, Daisuke. / Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA. :: EMBO Journal. 2007 ; 巻 26, 番号 10. pp. 2584-2593.
@article{eb864efbda824172a08d63e2c04de9f6,
title = "Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA",
abstract = "In eubacteria, PriA helicase detects the stalled DNA replication forks. This critical role of PriA is ascribed to its ability to bind to the 3′ end of a nascent leading DNA strand in the stalled replication forks. The crystal structures in complexes with oligonucleotides and the combination of fluorescence correlation spectroscopy and mutagenesis reveal that the N-terminal domain of PriA possesses a binding pocket for the 3′-terminal nucleotide residue of DNA. The interaction with the deoxyribose 3′-OH is essential for the 3′-terminal recognition. In contrast, the direct interaction with 3′-end nucleobase is unexpected, considering the same affinity for oligonucleotides carrying the four bases at the 3′ end. Thus, the N-terminal domain of PriA recognizes the 3′-end base in a base-non-selective manner, in addition to the deoxyribose and 5′-side phosphodiester group, of the 3′-terminal nucleotide to acquire both sufficient affinity and non-selectivity to find all of the stalled replication forks generated during DNA duplication. This unique feature is prerequisite for the proper positioning of the helicase domain of PriA on the unreplicated double-stranded DNA.",
author = "Kaori Tabata and Toyoyuki Ose and Naoaki Okamoto and Katsumi Maenaka and Taku Tanaka and Hisao Masai and Mihoko Saito and Tsuyoshi Shirai and Daisuke Kohda",
year = "2007",
month = "5",
day = "16",
doi = "10.1038/sj.emboj.7601697",
language = "English",
volume = "26",
pages = "2584--2593",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "10",

}

TY - JOUR

T1 - Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA

AU - Tabata, Kaori

AU - Ose, Toyoyuki

AU - Okamoto, Naoaki

AU - Maenaka, Katsumi

AU - Tanaka, Taku

AU - Masai, Hisao

AU - Saito, Mihoko

AU - Shirai, Tsuyoshi

AU - Kohda, Daisuke

PY - 2007/5/16

Y1 - 2007/5/16

N2 - In eubacteria, PriA helicase detects the stalled DNA replication forks. This critical role of PriA is ascribed to its ability to bind to the 3′ end of a nascent leading DNA strand in the stalled replication forks. The crystal structures in complexes with oligonucleotides and the combination of fluorescence correlation spectroscopy and mutagenesis reveal that the N-terminal domain of PriA possesses a binding pocket for the 3′-terminal nucleotide residue of DNA. The interaction with the deoxyribose 3′-OH is essential for the 3′-terminal recognition. In contrast, the direct interaction with 3′-end nucleobase is unexpected, considering the same affinity for oligonucleotides carrying the four bases at the 3′ end. Thus, the N-terminal domain of PriA recognizes the 3′-end base in a base-non-selective manner, in addition to the deoxyribose and 5′-side phosphodiester group, of the 3′-terminal nucleotide to acquire both sufficient affinity and non-selectivity to find all of the stalled replication forks generated during DNA duplication. This unique feature is prerequisite for the proper positioning of the helicase domain of PriA on the unreplicated double-stranded DNA.

AB - In eubacteria, PriA helicase detects the stalled DNA replication forks. This critical role of PriA is ascribed to its ability to bind to the 3′ end of a nascent leading DNA strand in the stalled replication forks. The crystal structures in complexes with oligonucleotides and the combination of fluorescence correlation spectroscopy and mutagenesis reveal that the N-terminal domain of PriA possesses a binding pocket for the 3′-terminal nucleotide residue of DNA. The interaction with the deoxyribose 3′-OH is essential for the 3′-terminal recognition. In contrast, the direct interaction with 3′-end nucleobase is unexpected, considering the same affinity for oligonucleotides carrying the four bases at the 3′ end. Thus, the N-terminal domain of PriA recognizes the 3′-end base in a base-non-selective manner, in addition to the deoxyribose and 5′-side phosphodiester group, of the 3′-terminal nucleotide to acquire both sufficient affinity and non-selectivity to find all of the stalled replication forks generated during DNA duplication. This unique feature is prerequisite for the proper positioning of the helicase domain of PriA on the unreplicated double-stranded DNA.

UR - http://www.scopus.com/inward/record.url?scp=34249071349&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34249071349&partnerID=8YFLogxK

U2 - 10.1038/sj.emboj.7601697

DO - 10.1038/sj.emboj.7601697

M3 - Article

VL - 26

SP - 2584

EP - 2593

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 10

ER -