Structural study of the archaeal homologous recombinant protein complexed with DNA fragments.
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.
Naoe
Chieko
C
School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa, Tokyo 142-8555, Japan.
Tsunoda
Masaru
M
Nakamura
Kazuo T
KT
D019843:Archaeal Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D002850:Chromatography, Gel; D003460:Crystallization; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D004058:Diffusion; D011485:Protein Binding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D016944:Sulfolobus / Q000737:chemistry*; D014835:Volatilization
D019843:Archaeal Proteins; D004268:DNA-Binding Proteins; C117252:RadA protein, archaeal; D011994:Recombinant Proteins; D004247:DNA