9FA4
Structure of the Integrator arm module containing subunits INTS10/13/14/15 (state 1)
Summary for 9FA4
Entry DOI | 10.2210/pdb9fa4/pdb |
Related | 9EOC 9EP1 |
EMDB information | 50267 |
Descriptor | Integrator complex subunit 15, Integrator complex subunit 10, Integrator complex subunit 13, ... (4 entities in total) |
Functional Keywords | integrator complex assembly, rna polymerase ii transcription termination, transcription factors, transcription |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 4 |
Total formula weight | 270314.00 |
Authors | Razew, M.,Galej, W.P. (deposition date: 2024-05-10, release date: 2024-06-12, Last modification date: 2024-07-24) |
Primary citation | Razew, M.,Fraudeau, A.,Pfleiderer, M.M.,Linares, R.,Galej, W.P. Structural basis of the Integrator complex assembly and association with transcription factors. Mol.Cell, 84:2542-, 2024 Cited by PubMed Abstract: Integrator is a multi-subunit protein complex responsible for premature transcription termination of coding and non-coding RNAs. This is achieved via two enzymatic activities, RNA endonuclease and protein phosphatase, acting on the promoter-proximally paused RNA polymerase Ⅱ (RNAPⅡ). Yet, it remains unclear how Integrator assembly and recruitment are regulated and what the functions of many of its core subunits are. Here, we report the structures of two human Integrator sub-complexes: INTS10/13/14/15 and INTS5/8/10/15, and an integrative model of the fully assembled Integrator bound to the RNAPⅡ paused elongating complex (PEC). An in silico protein-protein interaction screen of over 1,500 human transcription factors (TFs) identified ZNF655 as a direct interacting partner of INTS13 within the fully assembled Integrator. We propose a model wherein INTS13 acts as a platform for the recruitment of TFs that could modulate the stability of the Integrator's association at specific loci and regulate transcription attenuation of the target genes. PubMed: 38823386DOI: 10.1016/j.molcel.2024.05.009 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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