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7OOP

Pol II-CSB-CSA-DDB1-UVSSA-PAF-SPT6 (Structure 3)

Summary for 7OOP
Entry DOI10.2210/pdb7oop/pdb
EMDB information13010
DescriptorDNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, RNA_pol_L_2 domain-containing protein, ... (28 entities in total)
Functional Keywordstranscription, dna repair, tcr
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains26
Total formula weight1548140.36
Authors
Kokic, G.,Cramer, P. (deposition date: 2021-05-28, release date: 2021-10-06, Last modification date: 2024-07-17)
Primary citationKokic, G.,Wagner, F.R.,Chernev, A.,Urlaub, H.,Cramer, P.
Structural basis of human transcription-DNA repair coupling.
Nature, 598:368-372, 2021
Cited by
PubMed Abstract: Transcription-coupled DNA repair removes bulky DNA lesions from the genome and protects cells against ultraviolet (UV) irradiation. Transcription-coupled DNA repair begins when RNA polymerase II (Pol II) stalls at a DNA lesion and recruits the Cockayne syndrome protein CSB, the E3 ubiquitin ligase, CRL4 and UV-stimulated scaffold protein A (UVSSA). Here we provide five high-resolution structures of Pol II transcription complexes containing human transcription-coupled DNA repair factors and the elongation factors PAF1 complex (PAF) and SPT6. Together with biochemical and published data, the structures provide a model for transcription-repair coupling. Stalling of Pol II at a DNA lesion triggers replacement of the elongation factor DSIF by CSB, which binds to PAF and moves upstream DNA to SPT6. The resulting elongation complex, EC, uses the CSA-stimulated translocase activity of CSB to pull on upstream DNA and push Pol II forward. If the lesion cannot be bypassed, CRL4 spans over the Pol II clamp and ubiquitylates the RPB1 residue K1268, enabling recruitment of TFIIH to UVSSA and DNA repair. Conformational changes in CRL4 lead to ubiquitylation of CSB and to release of transcription-coupled DNA repair factors before transcription may continue over repaired DNA.
PubMed: 34526721
DOI: 10.1038/s41586-021-03906-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

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