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

Ming Hui Lee, Chih Hsiang Leng, Yuan Chih Chang, Chia Cheng Chou, Yi Kai Chen, Fu Fei Hsu, Chia Seng Chang, Andrew H.J. Wang, Ting Fang Wang

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17 引文 斯高帕斯(Scopus)


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 μm in length (∼10 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.

頁(從 - 到)845-851
期刊Biochemical and Biophysical Research Communications
出版狀態已發佈 - 10月 22 2004

ASJC Scopus subject areas

  • 生物物理學
  • 生物化學
  • 分子生物學
  • 細胞生物學


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