Egner C, Azhderian E, Tsang S S, Radding C M, Chase J W
J Bacteriol. 1987 Aug;169(8):3422-8. doi: 10.1128/jb.169.8.3422-3428.1987.
To relate the roles of Escherichia coli SSB in recombination in vivo and in vitro, we have studied the mutant proteins SSB-1 and SSB-113, the variant SSBc produced by chymotryptic cleavage, the partially homologous variant F SSB (encoded by the E. coli sex factor), and the protein encoded by gene 32 of bacteriophage T4. All of these, with the exception of SSB-1, augmented both the initial rate of homologous pairing and strand exchange promoted by RecA protein. From these and related observations, we conclude that SSB stimulates the initial formation of joint molecules by nonspecifically promoting the binding of RecA protein to single-stranded DNA; that SSB plays no role in synapsis of the RecA nucleoprotein filament with duplex DNA; that stimulation of strand exchange by SSB is similarly nonspecific; and that all members of the class of proteins represented by SSB, F SSB, and gene 32 protein may play equivalent roles in making single-stranded DNA more accessible to RecA protein.
为了阐明大肠杆菌单链结合蛋白(SSB)在体内和体外重组中的作用,我们研究了突变蛋白SSB-1和SSB-113、经胰凝乳蛋白酶切割产生的变体SSBc、部分同源变体F SSB(由大肠杆菌性因子编码)以及噬菌体T4基因32编码的蛋白。除了SSB-1之外,所有这些蛋白都提高了RecA蛋白促进的同源配对和链交换的初始速率。基于这些以及相关观察结果,我们得出以下结论:SSB通过非特异性促进RecA蛋白与单链DNA的结合来刺激接头分子的初始形成;SSB在RecA核蛋白丝与双链DNA的联会中不起作用;SSB对链交换的刺激同样是非特异性的;并且由SSB、F SSB和基因32蛋白代表的这类蛋白的所有成员在使单链DNA更易被RecA蛋白接近方面可能发挥同等作用。