Molecular basis for the interaction between Integrator subunits IntS9 and IntS11 and its functional importance Article Swipe
YOU?
·
· 2017
· Open Access
·
· DOI: https://doi.org/10.1073/pnas.1616605114
· OA: W2606817248
Significance The Integrator complex (INT) has important functions in the 3′-end processing of noncoding RNAs and RNA polymerase II transcription. The INT contains at least 14 subunits, but its molecular mechanism of action is still poorly understood. The endonuclease activity of INT is mediated by its subunit 11 (IntS11), which forms a stable complex with Integrator complex subunit 9 (IntS9) through their C-terminal domains (CTDs). Here, we report the crystal structure of the IntS9–IntS11 CTD complex at 2.1-Å resolution and detailed, structure-based biochemical and functional studies. Highly conserved residues are located in the extensive interface between the two CTDs. Yeast two-hybrid assays and coimmunoprecipitation experiments confirm the structural observations. Functional studies demonstrate that the IntS9–IntS11 interaction is crucial for INT in snRNA 3′-end processing.
