Structural Biology Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro 3, Madrid 28029, Spain.
Structural Biology Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro 3, Madrid 28029, Spain.
Curr Opin Struct Biol. 2021 Apr;67:78-85. doi: 10.1016/j.sbi.2020.08.010. Epub 2020 Oct 28.
RUVBL1 and RUVBL2 are two highly conserved AAA+ ATPases that form a hetero-hexameric complex that participates in a wide range of unrelated cellular processes, including chromatin remodeling, Fanconi Anemia (FA), nonsense-mediated mRNA decay (NMD), and assembly and maturation of several large macromolecular complexes such as RNA polymerases, the box C/D small nucleolar ribonucleoprotein (snoRNP) and mTOR complexes. How the RUVBL1-RUVBL2 complex works in such a variety of processes, sometimes antagonistic, has been obscure for a long time. Recent cryo-electron microscopy (cryo-EM) studies have started to reveal how RUVBL1-RUVBL2 forms a scaffold for complex protein-protein interactions and how the structure and ATPase activity of RUVBL1-RUVBL2 can be affected and regulated by the interaction with clients.
RUVBL1 和 RUVBL2 是两种高度保守的 AAA+ ATP 酶，它们形成一个异六聚体复合物，参与广泛的不相关的细胞过程，包括染色质重塑、范可尼贫血（FA）、无意义介导的 mRNA 降解（NMD），以及几种大型大分子复合物的组装和成熟，如 RNA 聚合酶、框 C/D 小核仁核糖核蛋白（snoRNP）和 mTOR 复合物。RUVBL1-RUVBL2 复合物在如此多种过程中发挥作用，有时是拮抗的，这在很长一段时间里一直不清楚。最近的低温电子显微镜（cryo-EM）研究开始揭示 RUVBL1-RUVBL2 如何形成一个复杂的蛋白质-蛋白质相互作用的支架，以及 RUVBL1-RUVBL2 的结构和 ATP 酶活性如何受到与客户相互作用的影响和调节。
