7OKX

Structure of active transcription elongation complex Pol II-DSIF (SPT5-KOW5)-ELL2-EAF1 (composite structure)

Summary for 7OKX

• Entry DOI: 10.2210/pdb7okx/pdb
• Related: 7OKX 7OKY 7OL0
• EMDB information: 12966 12967 12968 12969 12970 12971 12972 12973 12974
• Descriptor: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, RNA_pol_L_2 domain-containing protein, ... (20 entities in total)
• Functional Keywords: pol ii, super elongation complex, ell2, eaf1, transcription
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 18
• Total formula weight: 798288.07

Authors

Chen, Y.,Vos, S.M.,Dienemann, C.,Ninov, M.,Urlaub, H.,Cramer, P. (deposition date: 2021-05-18, release date: 2021-07-14, Last modification date: 2024-07-10)

Primary citation

Chen, Y.,Vos, S.M.,Dienemann, C.,Ninov, M.,Urlaub, H.,Cramer, P.
Allosteric transcription stimulation by RNA polymerase II super elongation complex.
Mol.Cell, 81:3386-3399.e10, 2021

PubMed Abstract: The super elongation complex (SEC) contains the positive transcription elongation factor b (P-TEFb) and the subcomplex ELL2-EAF1, which stimulates RNA polymerase II (RNA Pol II) elongation. Here, we report the cryoelectron microscopy (cryo-EM) structure of ELL2-EAF1 bound to a RNA Pol II elongation complex at 2.8 Å resolution. The ELL2-EAF1 dimerization module directly binds the RNA Pol II lobe domain, explaining how SEC delivers P-TEFb to RNA Pol II. The same site on the lobe also binds the initiation factor TFIIF, consistent with SEC binding only after the transition from transcription initiation to elongation. Structure-guided functional analysis shows that the stimulation of RNA elongation requires the dimerization module and the ELL2 linker that tethers the module to the RNA Pol II protrusion. Our results show that SEC stimulates elongation allosterically and indicate that this stimulation involves stabilization of a closed conformation of the RNA Pol II active center cleft.

PubMed: 34265249
DOI: 10.1016/j.molcel.2021.06.019

Experimental method

ELECTRON MICROSCOPY (3.3 Å)