Abstract
EVL is a member of the ENA/VASP family, which is involved in actin-remodeling processes. Previously, we reported that human EVL directly interacts with RAD51, which is an essential protein in the homologous recombinational repair of DNA double-strand breaks, and stimulates RAD51-mediated recombination reactions in vitro. To identify the EVL domain required for the recombination function, we purified the EVL fragments EVL(1-221) and EVL(222-418), which contain the EVH1 and Pro-rich domains and the EVH2 domain, respectively. We found that EVL(222-418) possesses DNA-binding and RAD51-binding activities, and also stimulates RAD51-mediated homologous pairing. In contrast, EVL(1-221) did not exhibit any of these activities. Therefore, the EVH2 domain, which is highly conserved among the ENA/VASP family proteins, may be responsible for the recombination function of EVL.
| Original language | English |
|---|---|
| Pages (from-to) | 5841-5848 |
| Number of pages | 8 |
| Journal | FEBS Journal |
| Volume | 276 |
| Issue number | 20 |
| DOIs | |
| Publication status | Published - 2009 Oct |
Fingerprint
Keywords
- DSB
- ENA/VASP
- EVL
- Homologous recombination
- RAD51
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
Biochemical analysis of the human EVL domains in homologous recombination. / Takaku, Motoki; MacHida, Shinichi; Nakayama, Shugo; Takahashi, Daisuke; Kurumizaka, Hitoshi.
In: FEBS Journal, Vol. 276, No. 20, 10.2009, p. 5841-5848.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Biochemical analysis of the human EVL domains in homologous recombination
AU - Takaku, Motoki
AU - MacHida, Shinichi
AU - Nakayama, Shugo
AU - Takahashi, Daisuke
AU - Kurumizaka, Hitoshi
PY - 2009/10
Y1 - 2009/10
N2 - EVL is a member of the ENA/VASP family, which is involved in actin-remodeling processes. Previously, we reported that human EVL directly interacts with RAD51, which is an essential protein in the homologous recombinational repair of DNA double-strand breaks, and stimulates RAD51-mediated recombination reactions in vitro. To identify the EVL domain required for the recombination function, we purified the EVL fragments EVL(1-221) and EVL(222-418), which contain the EVH1 and Pro-rich domains and the EVH2 domain, respectively. We found that EVL(222-418) possesses DNA-binding and RAD51-binding activities, and also stimulates RAD51-mediated homologous pairing. In contrast, EVL(1-221) did not exhibit any of these activities. Therefore, the EVH2 domain, which is highly conserved among the ENA/VASP family proteins, may be responsible for the recombination function of EVL.
AB - EVL is a member of the ENA/VASP family, which is involved in actin-remodeling processes. Previously, we reported that human EVL directly interacts with RAD51, which is an essential protein in the homologous recombinational repair of DNA double-strand breaks, and stimulates RAD51-mediated recombination reactions in vitro. To identify the EVL domain required for the recombination function, we purified the EVL fragments EVL(1-221) and EVL(222-418), which contain the EVH1 and Pro-rich domains and the EVH2 domain, respectively. We found that EVL(222-418) possesses DNA-binding and RAD51-binding activities, and also stimulates RAD51-mediated homologous pairing. In contrast, EVL(1-221) did not exhibit any of these activities. Therefore, the EVH2 domain, which is highly conserved among the ENA/VASP family proteins, may be responsible for the recombination function of EVL.
KW - DSB
KW - ENA/VASP
KW - EVL
KW - Homologous recombination
KW - RAD51
UR - http://www.scopus.com/inward/record.url?scp=70349496097&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70349496097&partnerID=8YFLogxK
U2 - 10.1111/j.1742-4658.2009.07265.x
DO - 10.1111/j.1742-4658.2009.07265.x
M3 - Article
C2 - 19725871
AN - SCOPUS:70349496097
VL - 276
SP - 5841
EP - 5848
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 20
ER -