A new paper on the Integrator complex
Our newest paper describing the structure of the catalytic core of the Integrator complex is online now in Molecular Cell.
Integrator complex was discovered more than 15 years ago as a specialised endonuclease responsible for the 3’-end processing of spliceosomal snRNAs. More recent studies provided compelling evidence that it is involved in genome-wide transcription attenuation of thousands of transcripts from different classes.
Using cell biology and proteomics, Moritz Pfleiderer identified stable modules within this complex, expressed them recombinantly and determined the structure of one of them by cryo-EM.
The structure provides new insights into the arrangement and assembly mechanism of the catalytic nuclease heterodimer, INTS9/11, and the recruitment of a helical protein INTS4. All three proteins form a charged cavity, which is likely involved in guiding RNA towards the endonuclease active site.
Comparison with the related CPSF complex shows some interesting differences in the spatial organisation of the two complexes.