晨间信号Morning Signal
《科学》 第391卷 第6788期 · 2026年2月26日 · 中文解读

冷冻电镜揭示RAD51丝状组装及XRCC3复合物封端机制

Cryo–electron microscopic visualization of RAD51 filament assembly and end-capping by XRCC3-RAD51C-RAD51D-XRCC2 · L. A. Greenhough et al.
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本研究通过冷冻电镜和单分子成像揭示了XRCC3-RAD51C-RAD51D-XRCC2复合物在RAD51丝状组装和封端中的结构与功能,并发现其与RAD51B复合物在进化上保守的机制。
原文开头
Full article and list of author affiliations: https://doi.org/10.1126/ science.aea1546 Luke A. Greenhough*, Lorenzo Galanti, Chih-Chao Liang, Simon J. Boulton, Stephen C. West* INTRODUCTION: Homologous recombination safeguards genome stability by repairing DNA double-strand breaks. Central to this process is RAD51 protein, which polymerizes on single-stranded DNA (ssDNA) to pair homologous sequences with the sister chromatid. In humans, five RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, and XRCC3) support this process, although their precise roles are not fully understood. RAD51 paralog knockouts in mice are embryonic lethal, and in human cells, depletion impairs RAD51 foci formation, increases genotoxic sensitivity, and causes growth defects. Notably, these genes are linked to cancer predisposition and Fanconi anemia. …
摘自《科学》(Science)第391卷 第6788期 · 2026年2月26日,L. A. Greenhough et al.。仅引用开头一小段供了解文章,版权归原刊所有,全文请阅读原刊。
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