Lineberger Comprehensive Cancer Center, and Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Nucleic Acids Res. 2013 Jun;41(11):5927-37. doi: 10.1093/nar/gkt266. Epub 2013 Apr 19.
Infected cell protein 8 (ICP8) from herpes simplex virus 1 was first identified as a single-strand (ss) DNA-binding protein. It is essential for, and abundant during, viral replication. Studies in vitro have shown that ICP8 stimulates model replication reactions, catalyzes annealing of complementary ssDNAs and, in combination with UL12 exonuclease, will catalyze ssDNA annealing homologous recombination. DNA annealing and strand transfer occurs within large oligomeric filaments of ssDNA-bound ICP8. We present the first 3D reconstruction of a novel ICP8-ssDNA complex, which seems to be the basic unit of the DNA annealing machine. The reconstructed volume consists of two nonameric rings containing ssDNA stacked on top of each other, corresponding to a molecular weight of 2.3 MDa. Fitting of the ICP8 crystal structure suggests a mechanism for the annealing reaction catalyzed by ICP8, which is most likely a general mechanism for protein-driven DNA annealing.
单纯疱疹病毒 1 的感染细胞蛋白 8（ICP8）最初被鉴定为单链（ss）DNA 结合蛋白。它是病毒复制所必需的，并且在病毒复制期间丰富。体外研究表明，ICP8 刺激模型复制反应，催化互补 ssDNA 的退火，并且与 UL12 核酸外切酶结合，将催化 ssDNA 退火同源重组。DNA 退火和链转移发生在 ssDNA 结合的 ICP8 的大型寡聚丝中。我们提出了新型 ICP8-ssDNA 复合物的第一个 3D 重建，它似乎是 DNA 退火机器的基本单元。重建的体积由两个非环状 ssDNA 组成，彼此堆叠，分子量为 2.3 MDa。ICP8 晶体结构的拟合表明了 ICP8 催化的退火反应的机制，这很可能是一种用于蛋白驱动的 DNA 退火的通用机制。
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