Polosa P L, Roberti M, Mustich A, Gadaleta M N, Cantatore P
Dipartimento di Biochimica e Biologia Molecolare, Università di Bari, Italy.
Curr Genet. 1994 Apr;25(4):350-6. doi: 10.1007/BF00351489.
A mitochondrial protein, able to specifically bind two double-stranded homologous sequences of sea-urchin mitochondrial DNA, has been partially purified from Paracentrotus lividus eggs. This protein, present at a low concentration, is a polypeptide of 40 kDa. One of the binding sequences, located in the main non-coding region, contains the replication origin of the mitochondrial DNA H-strand. By a combination of band-shift, DNase footprinting, and modification interference analyses with homologous and heterologous probes we identified YCYYATCAN(A/T)RC as the minimum sequence required for the binding. The protein also shows a single-stranded DNA-binding activity, as it is able to specifically interact with one of the strands of the binding sites. These features are consistent with a function of the protein in the modulation of sea-urchin mitochondrial DNA replication during the development stages.
一种能够特异性结合海胆线粒体DNA两条双链同源序列的线粒体蛋白已从地中海海胆卵中部分纯化出来。这种蛋白浓度较低，是一种40 kDa的多肽。其中一个结合序列位于主要非编码区，包含线粒体DNA H链的复制起点。通过结合使用带移分析、DNA酶足迹分析以及对同源和异源探针的修饰干扰分析，我们确定YCYYATCAN(A/T)RC为结合所需的最小序列。该蛋白还表现出单链DNA结合活性，因为它能够与结合位点的其中一条链特异性相互作用。这些特性与该蛋白在海胆发育阶段调节线粒体DNA复制中的功能相一致。
