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首页> 外文期刊>Journal of Molecular Biology >The bipolar filaments formed by herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing.
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The bipolar filaments formed by herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing.

机译：由1型单纯疱疹病毒SSB /重组蛋白（ICP8）形成的双极细丝提示了DNA退火的机制。

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摘要

Herpes simplex virus type 1 encodes a multifunctional protein, ICP8, which serves both as a single-strand binding protein and as a recombinase, catalyzing reactions involved in replication and recombination of the viral genome. In the presence of divalent ions and at low temperature, previous electron microscopic studies showed that ICP8 will form long left-handed helical filaments. Here, electron microscopic image reconstruction reveals that the filaments are bipolar, with an asymmetric unit containing two subunits of ICP8 that constitute a symmetrical dimer. This organization of the filament has been confirmed using scanning transmission electron microscopy. The pitch of the filaments is approximately 250 A, with approximately 6.2 dimers per turn. Docking of a crystal structure of ICP8 into the reconstructed filament shows that the C-terminal domain of ICP8, attached to the body of the subunit by a flexible linker containing approximately 10 residues, is packed into a pocket in the body of a neighboring subunit in the crystal in a similar manner as in the filament. However, the interactions between the large N-terminal domains are quite different in the filament from that observed in the crystal. A previously proposed model for ICP8 binding single-stranded DNA (ssDNA), based upon the crystal structure, leads to a model for a continuous strand of ssDNA near the filament axis. The bipolar nature of the ICP8 filaments means that a second strand of ssDNA would be running through this filament in the opposite orientation, and this provides a potential mechanism for how ICP8 anneals complementary ssDNA into double-stranded DNA, where each strand runs in opposite directions.
机译：1型单纯疱疹病毒编码多功能蛋白ICP8，它既充当单链结合蛋白又充当重组酶，催化病毒基因组复制和重组中涉及的反应。在存在二价离子且温度较低的情况下，先前的电子显微镜研究表明ICP8将形成长的左手螺旋丝。在此，电子显微镜图像重建揭示了细丝是双极性的，其不对称单元包含构成对称二聚体的两个ICP8亚基。细丝的这种组织已经使用扫描透射电子显微镜确认。灯丝的螺距约为250 A，每匝约6.2二聚体。将ICP8的晶体结构对接到重建的细丝中，表明ICP8的C端结构域通过包含约10个残基的柔性连接子连接到该亚基的主体，并被包装在一个相邻亚基的主体的口袋中。以类似于灯丝的方式形成晶体。但是，长丝中大的N端结构域之间的相互作用与晶体中观察到的完全不同。先前提出的基于晶体结构的ICP8结合单链DNA（ssDNA）的模型导致了在丝轴附近的ssDNA连续链的模型。 ICP8细丝的双极性性质意味着第二条ssDNA链将以相反的方向穿过该细丝，这为ICP8将互补ssDNA退火为双链DNA（每条链以相反的方向）提供了潜在的机制。 。

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