为了研究这一点，该课题组人员利用了黑腹果蝇的多蛋白复合物，该复合物保护端粒免受致命离子的侵害，尽管有一个亚基HOAP （HP1/ ORC相关蛋白），自适应地进化以限制自私的端粒反转录转座子。在亲缘关系密切的果蝇物种之间交换HOAP自适应进化的相互作用伙伴HipHop （HP1-HOAP相互作用蛋白），破坏了HOAP向端粒的募集，导致致命的端粒脱落。恢复HipHop与HOAP相互作用表面的6个自适应进化位点，或引入其同源HOAP，恢复蛋白质募集、端粒保护和生存能力。它们在体内以进化为导向的操作阐明了分子间代偿进化如何在面对自私元素的对抗时保持基本功能。
据悉，基因组内与自私遗传元件的冲突刺激了必需多蛋白复合物亚基的适应性变化。这些适应性变化是否以及如何破坏这些复合体内部的相互作用并威胁到它们的基本功能仍未得到探索。
附：英文原文
Title: Rapid compensatory evolution within a multiprotein complex preserves telomere integrity
Author: Sung-Ya Lin, Hannah R. Futeran, Briana N. Cruga, Andrew Santiago-Frangos, Mia T. Levine
Issue&Volume: 2025-11-27
Abstract: Intragenomic conflict with selfish genetic elements spurs adaptive changes in subunits of essential multiprotein complexes. Whether and how these adaptive changes disrupt interactions within such complexes and threaten their essential functions remains unexplored. To investigate this, we exploited a Drosophila melanogaster multiprotein complex that protects telomeres from lethal fusions despite one subunit, HOAP (HP1/ORC–associated protein), evolving adaptively to restrict selfish telomeric retrotransposons. Swapping HOAP’s adaptively evolving interaction partner, HipHop (HP1-HOAP–interacting protein), between closely related Drosophila species disrupted HOAP recruitment to the telomere, leading to lethal telomere fusions. Reverting six adaptively evolving sites on HipHop’s interaction surface with HOAP, or introducing its conspecific HOAP, restored protein recruitment, telomere protection, and viability. Our in vivo, evolution-guided manipulations illuminate how intermolecular compensatory evolution preserves essential functions in the face of antagonism by selfish elements.
DOI: adv0657
Source: https://www.science.org/doi/10.1126/science.adv0657