1) The multi-subunit exosome complex is a key player in RNA quality control systems of eukaryotic cells. In order to fully understand the mechanisms and regulations of this important cellular machinery, we utilize cryo-EM and single particle reconstruction techniques to capture clear snapshots of the entire exosome complex binding with its different cofactors in various working states.
2) Recently, we used single-particle cryo-electron microscopy to solve the structures of
the Ski7-exosome complex in RNA-free and RNA-bound forms at resolutions of 4.2 Å and 5.8 Å, respectively. These structures revealed that the N-terminal domain of Ski7 adopts a structural arrangement and interacts with the exosome in a similar fashion to the nuclear Rrp6’s C-terminal domain. Further structural analysis of the exosome with different RNAs suggests a switch mechanism of RNA-induced exosome’s activation in through-core RNA processing.