Characterization of the oligomeric states of RecA protein: Monomeric RecA protein can form a nucleoprotein filament

被引：18

作者：

Masui, R ^{[1
]}

Mikawa, T ^{[1
]}

Kato, R ^{[1
]}

Kuramitsu, S ^{[1
]}

机构：

[1] Osaka Univ, Grad Sch Sci, Dept Biol, Osaka 5600043, Japan

来源：

BIOCHEMISTRY | 1998年 / 37卷 / 42期

关键词：

D O I：

10.1021/bi981296c

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Self-assembly of RecA protein in solution and on single-stranded DNA exerts a significant effect on the catalytic activities of this protein. To manipulate the self-association reaction, we examined the effects of various salts on the self-association of RecA from Thermus thermophilus (ttRecA) by circular dichroism spectroscopy and gel-filtration analysis. We showed that the self-association of ttRecA strongly depends on the kind and concentration of the salt, as well as on the protein concentration. Chaotropic ions were especially useful for obtaining RecA in its hexameric and monomeric states. On the basis of these observations, we were able to regulate the oligomeric states of ttReca and we then examined the activity of RecA in various oligomeric states. Monomeric ttRecA bound to ssDNA and formed a nucleoprotein filament, which showed ssDNA-dependent ATPase activity. These results suggest that the monomeric form of RecA is an intermediate in filament formation on ssDNA.

引用

页码：14788 / 14797

页数：10