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首页> 外文期刊>Biochemistry >Single-Stranded DNA Binding Proteins Unwind the Newly Synthesized Double-Stranded DNA of Model Miniforks
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Single-Stranded DNA Binding Proteins Unwind the Newly Synthesized Double-Stranded DNA of Model Miniforks

机译：单链DNA结合蛋白可解开Miniforks模型的新合成双链DNA

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摘要

Single-stranded DNA binding (SSB) proteins are essential proteins of DNA metabolism. We characterized the binding of the bacteriophage T4 SSB, Escherichia coil SSB, human replication protein A (hRPA), and human hSSB1 proteins onto model miniforks and double-stranded single-stranded (ds-ss) junctions exposing 3' or 5' ssDNA overhangs. T4 SSB proteins, E. coil SSB proteins, and hRPA have a different binding preference for the ss tail exposed on model miniforks and ds-ss junctions. The T4 SSB protein preferentially binds substrates with 5' ss tails, whereas the E. coil SSB protein and hRPA show a preference for substrates with 3' ss overhangs. When interacting with ds-ss junctions or miniforks, the T4 SSB protein, E. coil SSB protein, and hRPA can destabilize not only the ds part of a ds-ss junction but also the daughter ds arm of a minifork. The T4 SSB protein displays these unwinding activities in a polar manner. Taken together, our results position the SSB protein as a potential key player in the reversal of a stalled replication fork and in gap repair-mediated repetitive sequence expansion.
机译：单链DNA结合（SSB）蛋白是DNA代谢必不可少的蛋白。我们表征了噬菌体T4 SSB，大肠杆菌线圈SSB，人类复制蛋白A（hRPA）和人类hSSB1蛋白到模型叉和暴露3'或5'ssDNA悬垂的双链单链（ds-ss）连接上的结合。 。 T4 SSB蛋白，大肠杆菌线圈SSB蛋白和hRPA对于暴露在模型迷你叉和ds-ss交界处的ss尾巴具有不同的结合偏好。 T4 SSB蛋白优先结合具有5'ss尾巴的底物，而大肠杆菌SSB蛋白质和hRPA显示出对具有3'ss突出端的底物的偏爱。当与ds-ss接头或迷你叉相互作用时，T4 SSB蛋白，大肠杆菌SSB蛋白和hRPA不仅会使ds-ss接头的ds部分不稳定，而且会使迷你叉的子ds臂不稳定。 T4 SSB蛋白以极性方式显示这些解旋活性。综上所述，我们的结果将SSB蛋白定位为逆转停滞的复制叉和缺口修复介导的重复序列扩增的潜在关键参与者。

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