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Title | Structure of the catalytic core of the Integrator complex. |
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Journal, issue, pages | Mol Cell, Vol. 81, Issue 6, Page 1246-11259.e8, Year 2021 |
Publish date | Mar 18, 2021 |
![]() | Moritz M Pfleiderer / Wojciech P Galej / ![]() |
PubMed Abstract | The Integrator is a specialized 3' end-processing complex involved in cleavage and transcription termination of a subset of nascent RNA polymerase II transcripts, including small nuclear RNAs (snRNAs) ...The Integrator is a specialized 3' end-processing complex involved in cleavage and transcription termination of a subset of nascent RNA polymerase II transcripts, including small nuclear RNAs (snRNAs). We provide evidence of the modular nature of the Integrator complex by biochemically characterizing its two subcomplexes, INTS5/8 and INTS10/13/14. Using cryoelectron microscopy (cryo-EM), we determined a 3.5-Å-resolution structure of the INTS4/9/11 ternary complex, which constitutes Integrator's catalytic core. Our structure reveals the spatial organization of the catalytic nuclease INTS11, bound to its catalytically impaired homolog INTS9 via several interdependent interfaces. INTS4, a helical repeat protein, plays a key role in stabilizing nuclease domains and other components. In this assembly, all three proteins form a composite electropositive groove, suggesting a putative RNA binding path within the complex. Comparison with other 3' end-processing machineries points to distinct features and a unique architecture of the Integrator's catalytic module. |
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Methods | EM (single particle) |
Resolution | 3.56 - 6.5 Å |
Structure data | ![]() EMDB-12159: ![]() EMDB-12163: ![]() EMDB-12164: EMDB-12165, PDB-7bfp: EMDB-12166: Medium resolution map of the Integrator cleavage module |
Source |
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![]() | NUCLEAR PROTEIN / Nuclease / Integrator / 3'-end processing |