Maria I. Dauden, AndrésLópez-Perrote & Oscar Llorca.
Abstract: 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.
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