Self-polymerization of archaeal RadA protein into long and fine helical filaments

被引：16
作者：
Lee, MH
Leng, CH
Chang, YC
Chou, CC
Chen, YK
Hsu, FF
Chang, CS
Wang, AHJ [1 ]
Wang, TF
机构：
[1] Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan
[2] Acad Sinica, Natl Core Facil High Throughput Prot Prod, Taipei 115, Taiwan
[3] Acad Sinica, Inst Phys, Taipei 115, Taiwan
[4] Acad Sinica, Natl Core Facil High Throughput Prot Crystallog, Taipei 115, Taiwan
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 323卷 / 03期
关键词：
RadA; homologous recombination; AFM; rad51; RecA; Dmc1;
D O I：
10.1016/j.bbrc.2004.08.163
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The Archaeal protein RadA, a RecA/Rad51 homolog, is able to promote pairing and exchange of DNA strands with homologous sequences. Here, we have expressed, purified, and crystallized the catalytically active RadA protein from Sulfolobus solfataricus (Sso). Preliminary X-ray analysis indicated that Sso RadA protein likely forms helical filament in protein crystals. Using atomic force microscopy with a carbon nanotube (CNT) tip for high-resolution imaging, we demonstrated that Sso RadA protein indeed forms fine helical filaments up to 1 mum in length (similar to10 nm pitch) in the absence of DNA and nucleotide cofactor. We also observed that Sso RadA protein helical filament could dissemble upon incubation with ssDNA, and then the proteins associate with ssDNA to form nucleoprotein filament. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码：845 / 851
页数：7
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