Department of Physiology and Biophysics and the Massey Cancer Center, Virginia Commonwealth University School of Medicine, Richmond, Virginia, USA.
J Biol Chem. 2020 Oct 23;295(43):14563-14564. doi: 10.1074/jbc.H120.016038.
Some plant proteases contain a latent sequence known as the plant-specific insert (PSI) that, upon release from the full protease sequence, initiates membrane fusion to defend from pathogens. However, the mechanism by which it exerts its effects has been unclear. Zhao report an elegant integration of biophysical experiments and molecular dynamics simulations to reveal events leading up to PSI-mediated membrane fusion. Their results demonstrate a pH-dependent monomer-to-dimer transition, clear evidence of membrane association, and probable structures of prefusion intermediates. These data expand our understanding of the elusive PSIs and may provide new directions for antimicrobial development.
一些植物蛋白酶含有一个潜在的序列，称为植物特异性插入（PSI），当从完整的蛋白酶序列中释放出来时，它会启动膜融合以抵御病原体。然而，其发挥作用的机制尚不清楚。Zhao 报告了一项将生物物理实验和分子动力学模拟相结合的精巧研究，揭示了导致 PSI 介导的膜融合的事件。他们的结果表明了 pH 依赖性的单体到二聚体的转变，这是膜结合的明确证据，并且可能是融合前中间体的结构。这些数据扩展了我们对难以捉摸的 PSI 的理解，并可能为抗菌药物的开发提供新的方向。
