@article{b58897020eb643e99bbaff82130ba8c2,
title = "Self-polymerization of archaeal RadA protein into long and fine helical filaments",
abstract = "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.",
keywords = "AFM, Dmc1, Homologous recombination, Rad51, RadA, RecA",
author = "Lee, \{Ming Hui\} and Leng, \{Chih Hsiang\} and Chang, \{Yuan Chih\} and Chou, \{Chia Cheng\} and Chen, \{Yi Kai\} and Hsu, \{Fu Fei\} and Chang, \{Chia Seng\} and Wang, \{Andrew H.J.\} and Wang, \{Ting Fang\}",
note = "Funding Information: This study was supported by grants from the National Science Council to T.-F. Wang (92-2311-B-001-055) and Academia Sinica (AS92IBC3) to A.H.-J. Wang. The National Core Facilities of High-Throughput Protein Production and Protein Crystallization were funded to A.H.-J. Wang by the National Genomic Medicine Project from National Science Council. We thank Dr. Igarashi and the staffs at Beamline BL18B of Photon Factory for the assistance of data collection. M.H. Lee and C.H. Leng contributed equally to this work.",
year = "2004",
month = oct,
day = "22",
doi = "10.1016/j.bbrc.2004.08.163",
language = "English",
volume = "323",
pages = "845--851",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier B.V.",
number = "3",
}