Abstract
The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a β-β-β-α fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the β-β-β-α fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.
| Original language | English |
|---|---|
| Pages (from-to) | 359-371 |
| Number of pages | 13 |
| Journal | Molecular Cell |
| Volume | 10 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2002 Aug |
| Externally published | Yes |
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ASJC Scopus subject areas
- Molecular Biology
Cite this
Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form. / Kagawa, Wataru; Kurumizaka, Hitoshi; Ishitani, Ryuichiro; Fukai, Shuya; Nureki, Osamu; Shibata, Takehiko; Yokoyama, Shigeyuki.
In: Molecular Cell, Vol. 10, No. 2, 08.2002, p. 359-371.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form
AU - Kagawa, Wataru
AU - Kurumizaka, Hitoshi
AU - Ishitani, Ryuichiro
AU - Fukai, Shuya
AU - Nureki, Osamu
AU - Shibata, Takehiko
AU - Yokoyama, Shigeyuki
PY - 2002/8
Y1 - 2002/8
N2 - The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a β-β-β-α fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the β-β-β-α fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.
AB - The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a β-β-β-α fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the β-β-β-α fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.
UR - http://www.scopus.com/inward/record.url?scp=0036671363&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036671363&partnerID=8YFLogxK
U2 - 10.1016/S1097-2765(02)00587-7
DO - 10.1016/S1097-2765(02)00587-7
M3 - Article
C2 - 12191481
AN - SCOPUS:0036671363
VL - 10
SP - 359
EP - 371
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 2
ER -