{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lin MH"],"funding":["U.S. Department of Health &amp; Human Services | NIH | National Institute of General Medical Sciences","NIGMS NIH HHS","Cancer Prevention and Research Institute of Texas","Kempner Predoctoral Fellowship"],"pagination":["5742"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9525679"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Integrator is a multi-subunit protein complex associated with RNA polymerase II (Pol II), with critical roles in noncoding RNA 3'-end processing and transcription attenuation of a broad collection of mRNAs. IntS11 is the endonuclease for RNA cleavage, as a part of the IntS4-IntS9-IntS11 Integrator cleavage module (ICM). Here we report a cryo-EM structure of the Drosophila ICM, at 2.74 Å resolution, revealing stable association of an inositol hexakisphosphate (IP<sub>6</sub>) molecule. The IP<sub>6</sub> binding site is located in a highly electropositive pocket at an interface among all three subunits of ICM, 55 Å away from the IntS11 active site and generally conserved in other ICMs. We also confirmed IP<sub>6</sub> association with the same site in human ICM. IP<sub>6</sub> binding is no"],"journal":["Nature communications"],"pubmed_title":["Inositol hexakisphosphate is required for Integrator function."],"pmcid":["PMC9525679"],"funding_grant_id":["R01 GM134539","R35 GM118093","R01GM134539","R35GM118093","T32 GM135134","RP170593"],"pubmed_authors":["Lin MH","Elrod ND","Huang KL","Tong L","Welle KA","Wagner EJ","Jensen MK"],"additional_accession":[]},"is_claimable":false,"name":"Inositol hexakisphosphate is required for Integrator function.","description":"Integrator is a multi-subunit protein complex associated with RNA polymerase II (Pol II), with critical roles in noncoding RNA 3'-end processing and transcription attenuation of a broad collection of mRNAs. IntS11 is the endonuclease for RNA cleavage, as a part of the IntS4-IntS9-IntS11 Integrator cleavage module (ICM). Here we report a cryo-EM structure of the Drosophila ICM, at 2.74 Å resolution, revealing stable association of an inositol hexakisphosphate (IP<sub>6</sub>) molecule. The IP<sub>6</sub> binding site is located in a highly electropositive pocket at an interface among all three subunits of ICM, 55 Å away from the IntS11 active site and generally conserved in other ICMs. We also confirmed IP<sub>6</sub> association with the same site in human ICM. IP<sub>6</sub> binding is no","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-06-01T02:10:27.84Z","creation":"2025-02-19T01:28:32.52Z"},"accession":"S-EPMC9525679","cross_references":{"pubmed":["36180473"],"doi":["10.1038/s41467-022-33506-3"]}}