Homologous pairing activities of Arabidopsis thaliana RAD51 and DMC1

Wataru Kobayashi; Enwei Liu; Hajime Ishii; Sachihiro Matsunaga; Peter Schlögelhofer; Hitoshi Kurumizaka

doi:10.1093/jb/mvy105

Homologous pairing activities of Arabidopsis thaliana RAD51 and DMC1

Wataru Kobayashi, Enwei Liu, Hajime Ishii, Sachihiro Matsunaga, Peter Schlögelhofer, Hitoshi Kurumizaka

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

In eukaryotes, homologous recombination plays a pivotal role in both genome maintenance and generation of genetic diversity. Eukaryotic RecA homologues, RAD51 and DMC1, are key proteins in homologous recombination that promote pairing between homologous DNA sequences. Arabidopsis thaliana is a prominent model plant for studying eukaryotic homologous recombination. However, A. thaliana RAD51 and DMC1 have not been biochemically characterized. In the present study, we purified A. thaliana RAD51 (AtRAD51) and DMC1 (AtDMC1). Biochemical analyses revealed that both AtRAD51 and AtDMC1 possess ATP hydrolyzing activity, filament formation activity and homologous pairing activity in vitro. We then compared the homologous pairing activities of AtRAD51 and AtDMC1 with those of the Oryza sativa and Homo sapiens RAD51 and DMC1 proteins.

Original language	English
Pages (from-to)	289-295
Number of pages	7
Journal	Journal of biochemistry
Volume	165
Issue number	3
DOIs	https://doi.org/10.1093/jb/mvy105
Publication status	Published - 2019 Mar 1

Keywords

Arabidopsis thaliana
DMC1
homologous pairing
homologous recombination
RAD51

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.1093/jb/mvy105

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abstract = "In eukaryotes, homologous recombination plays a pivotal role in both genome maintenance and generation of genetic diversity. Eukaryotic RecA homologues, RAD51 and DMC1, are key proteins in homologous recombination that promote pairing between homologous DNA sequences. Arabidopsis thaliana is a prominent model plant for studying eukaryotic homologous recombination. However, A. thaliana RAD51 and DMC1 have not been biochemically characterized. In the present study, we purified A. thaliana RAD51 (AtRAD51) and DMC1 (AtDMC1). Biochemical analyses revealed that both AtRAD51 and AtDMC1 possess ATP hydrolyzing activity, filament formation activity and homologous pairing activity in vitro. We then compared the homologous pairing activities of AtRAD51 and AtDMC1 with those of the Oryza sativa and Homo sapiens RAD51 and DMC1 proteins.",

keywords = "Arabidopsis thaliana, DMC1, homologous pairing, homologous recombination, RAD51",

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T1 - Homologous pairing activities of Arabidopsis thaliana RAD51 and DMC1

AU - Kobayashi, Wataru

AU - Liu, Enwei

AU - Ishii, Hajime

AU - Matsunaga, Sachihiro

AU - Schlögelhofer, Peter

AU - Kurumizaka, Hitoshi

PY - 2019/3/1

Y1 - 2019/3/1

N2 - In eukaryotes, homologous recombination plays a pivotal role in both genome maintenance and generation of genetic diversity. Eukaryotic RecA homologues, RAD51 and DMC1, are key proteins in homologous recombination that promote pairing between homologous DNA sequences. Arabidopsis thaliana is a prominent model plant for studying eukaryotic homologous recombination. However, A. thaliana RAD51 and DMC1 have not been biochemically characterized. In the present study, we purified A. thaliana RAD51 (AtRAD51) and DMC1 (AtDMC1). Biochemical analyses revealed that both AtRAD51 and AtDMC1 possess ATP hydrolyzing activity, filament formation activity and homologous pairing activity in vitro. We then compared the homologous pairing activities of AtRAD51 and AtDMC1 with those of the Oryza sativa and Homo sapiens RAD51 and DMC1 proteins.

AB - In eukaryotes, homologous recombination plays a pivotal role in both genome maintenance and generation of genetic diversity. Eukaryotic RecA homologues, RAD51 and DMC1, are key proteins in homologous recombination that promote pairing between homologous DNA sequences. Arabidopsis thaliana is a prominent model plant for studying eukaryotic homologous recombination. However, A. thaliana RAD51 and DMC1 have not been biochemically characterized. In the present study, we purified A. thaliana RAD51 (AtRAD51) and DMC1 (AtDMC1). Biochemical analyses revealed that both AtRAD51 and AtDMC1 possess ATP hydrolyzing activity, filament formation activity and homologous pairing activity in vitro. We then compared the homologous pairing activities of AtRAD51 and AtDMC1 with those of the Oryza sativa and Homo sapiens RAD51 and DMC1 proteins.

KW - Arabidopsis thaliana

KW - DMC1

KW - homologous pairing

KW - homologous recombination

KW - RAD51

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Homologous pairing activities of Arabidopsis thaliana RAD51 and DMC1

Abstract

Keywords

ASJC Scopus subject areas

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