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Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
Published on: December 17, 2016
Structural study of the archaeal homologous recombinant protein complexed with DNA fragments
Chieko Naoe1, Masaru Tsunoda, Kazuo T Nakamura
1School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa, Tokyo 142-8555, Japan.
Abstract:
RadA is involved in strand exchange reactions in homologous recombination which is a fundamental process in all organisms. Sulfolobus tokodaii, one of the archeabacteria, is an aerobic thermoacidophilic crenearchaeon which was isolated from hot springs. RadA from S. tokodaii (stRadA) is a heat resistance protein. The purified protein showed a single band on SDS-PAGE, and gel filtration analysis indicated that stRadA formed a multimeric structure. To reveal a mechanism of the homologous recombination at atomic resolution, stRadA was crystallized with DNA, and its crystals were obtained in 92 conditions by vapor-diffusion methods.
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