TY - JOUR
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
UR - http://www.scopus.com/inward/record.url?scp=85061992998&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85061992998&partnerID=8YFLogxK
U2 - 10.1093/jb/mvy105
DO - 10.1093/jb/mvy105
M3 - Article
C2 - 30517709
AN - SCOPUS:85061992998
SN - 0021-924X
VL - 165
SP - 289
EP - 295
JO - Journal of biochemistry
JF - Journal of biochemistry
IS - 3
ER -