Structural Basis Of The Rnamediated Retroneco2 Oligomerization Yanjing Wang Chen Wang Yongqi Yin Yongqing Cui Zhikang Dai Chang Liu Yanke Chen Zeyuan Guan Tingting Zou by Yanjing Wang & Chen Wang & Yongqi Yin & Yongqing Cui & Zhikang Dai & Chang Liu & Yanke Chen & Zeyuan Guan & Tingting Zou instant download after payment.

In the evolutionary arms race between bacteria and viruses, retrons have emerged as distinctive antiphage defense systems. Here,we elucidate the structure and function of Retron-Eco2, which comprises a non-coding RNA (ncRNA) that encodes multicopy singlestranded DNA (msDNA, a DNA‒RNA hybrid) and a fusion protein containing a reverse transcriptase (RT) domain and atopoisomerase-primase-like (Toprim) effector domain. The Eco2 msDNA and RT-Toprim fusion protein form a 1:1 stoichiometricnucleoprotein complex that further assembles into a trimer (msDNA:RT-Toprim ratio of 3:3) with a distinctive triangularconfiguration. The RNA portion of the msDNA in one protomer closely intertwines around the RT domain of an adjacent protomer,mediating the formation of this self-inhibitory assembly. Upon activation, the Toprim effector domain exhibits RNase activity,1234567890();,:degrading RNA to arrest phage replication. We further reveal that phage mutants evading Eco2-mediated defense harbormutations in the endonuclease IV-like protein DenB, underscoring DenB’s critical role in triggering the activation of this system.Together, these findings provide key structural and functional insights into Retron-Eco2, laying the groundwork for harnessing itspotential in biotechnology and synthetic biology applications.Cell Discovery;