Observation of RecA protein monomer by small angle X‐ray scattering with synchrotron radiation

FEBS Letters

Kamikubo, Hironari²  Kataoka, Mikio³  Kuramitsu, Seiki¹  Nakagawa, Noriko¹  Kato, Ryuichi¹  Mikawa, Tsutomu¹  Masui, Ryoji¹ 

[1] Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan;Institute of Materials Structure Science, High Energy Accelerator Research Organization, 1-1 Oho, Tsukuba, Ibaraki 305-0801, Japan;Laboratory of Bioenergetics and Biophysics, Graduate School of Materials Science, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama-cho, Ikoma, Nara 630-0101, Japan

关键词: RecA;    Oligomer;    Monomer;    Dissociation;    Small angle X-ray scattering;    Thermus thermophilus HB8;    SAXS;    small angle X-ray scattering;    CD;    circular dichroism;    BSA;    bovine serum albumin;   

DOI  :  10.1016/S0014-5793(00)02053-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

RecA protein is capable of forming homo-oligomers in solution. The oligomeric and monomeric states of Thermus thermophilus RecA protein were studied by small angle X-ray scattering, a direct method used to measure the overall dimensions of a macromolecule. In the presence of 3 M urea or 0.2 M lithium perchlorate, RecA dissociates from higher oligomeric states to form a hexamer with a radius of gyration (R _g) of 52 Å. The value of R _g decreased to 36 Å at a higher lithium perchlorate concentration (1.0 M). The zero angle intensity, I(0), was consistent with the identification of the former state as a hexamer and the latter as a monomer.

【 授权许可】

Unknown