Structural highlights
Function
INT9_HUMAN Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.
Publication Abstract from PubMed
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-A-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.
Structure of the catalytic core of the Integrator complex.,Pfleiderer MM, Galej WP Mol Cell. 2021 Mar 18;81(6):1246-1259.e8. doi: 10.1016/j.molcel.2021.01.005. Epub , 2021 Feb 5. PMID:33548203[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pfleiderer MM, Galej WP. Structure of the catalytic core of the Integrator complex. Mol Cell. 2021 Mar 18;81(6):1246-1259.e8. PMID:33548203 doi:10.1016/j.molcel.2021.01.005
