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TitleStructural basis of Integrator-mediated transcription regulation.
Journal, issue, pagesScience, Vol. 374, Issue 6569, Page 883-887, Year 2021
Publish dateNov 12, 2021
AuthorsIsaac Fianu / Ying Chen / Christian Dienemann / Olexandr Dybkov / Andreas Linden / Henning Urlaub / Patrick Cramer /
PubMed AbstractIntegrator and protein phosphatase 2A (PP2A) form a complex that dephosphorylates paused RNA polymerase II (Pol II), cleaves the nascent RNA, and terminates transcription. We report the structure of ...Integrator and protein phosphatase 2A (PP2A) form a complex that dephosphorylates paused RNA polymerase II (Pol II), cleaves the nascent RNA, and terminates transcription. We report the structure of the pretermination complex containing the human Integrator-PP2A complex bound to paused Pol II. Integrator binds Pol II and the pausing factors DSIF and NELF to exclude binding of the elongation factors SPT6 and PAF1 complex. Integrator also binds the C-terminal domain of Pol II and positions PP2A to counteract Pol II phosphorylation and elongation. The Integrator endonuclease docks to the RNA exit site and opens to cleave nascent RNA about 20 nucleotides from the Pol II active site. Integrator does not bind the DNA clamps formed by Pol II and DSIF, enabling release of DNA and transcription termination.
External linksScience / PubMed:34762484
MethodsEM (single particle)
Resolution3.6 Å
Structure data

13479

7pks

EMDB-13479, PDB-7pks:
Structural basis of Integrator-mediated transcription regulation
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-MN:
Unknown entry

Source
  • sus scrofa domesticus (domestic pig)
  • homo sapiens (human)
  • human immunodeficiency virus 1
KeywordsTRANSCRIPTION / Promoter proximal pausing / attenuation / snRNA termination / Integrator complex

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