5VVR

Ternary complex of RNA Pol II, transcription scaffold and Rad26

Summary for 5VVR

• Entry DOI: 10.2210/pdb5vvr/pdb
• Related: 5VVS
• EMDB information: 8735 8736 8737
• Descriptor: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11, ... (18 entities in total)
• Functional Keywords: complex, rna polymerase, csb, transcription, transcription-rna-dna complex, transcription/rna/dna
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 16
• Total formula weight: 671443.85

Authors

Lahiri, I.,Leschziner, A.E. (deposition date: 2017-05-19, release date: 2017-11-22, Last modification date: 2024-03-13)

Primary citation

Xu, J.,Lahiri, I.,Wang, W.,Wier, A.,Cianfrocco, M.A.,Chong, J.,Hare, A.A.,Dervan, P.B.,DiMaio, F.,Leschziner, A.E.,Wang, D.
Structural basis for the initiation of eukaryotic transcription-coupled DNA repair.
Nature, 551:653-657, 2017

PubMed Abstract: Eukaryotic transcription-coupled repair (TCR) is an important and well-conserved sub-pathway of nucleotide excision repair that preferentially removes DNA lesions from the template strand that block translocation of RNA polymerase II (Pol II). Cockayne syndrome group B (CSB, also known as ERCC6) protein in humans (or its yeast orthologues, Rad26 in Saccharomyces cerevisiae and Rhp26 in Schizosaccharomyces pombe) is among the first proteins to be recruited to the lesion-arrested Pol II during the initiation of eukaryotic TCR. Mutations in CSB are associated with the autosomal-recessive neurological disorder Cockayne syndrome, which is characterized by progeriod features, growth failure and photosensitivity. The molecular mechanism of eukaryotic TCR initiation remains unclear, with several long-standing unanswered questions. How cells distinguish DNA lesion-arrested Pol II from other forms of arrested Pol II, the role of CSB in TCR initiation, and how CSB interacts with the arrested Pol II complex are all unknown. The lack of structures of CSB or the Pol II-CSB complex has hindered our ability to address these questions. Here we report the structure of the S. cerevisiae Pol II-Rad26 complex solved by cryo-electron microscopy. The structure reveals that Rad26 binds to the DNA upstream of Pol II, where it markedly alters its path. Our structural and functional data suggest that the conserved Swi2/Snf2-family core ATPase domain promotes the forward movement of Pol II, and elucidate key roles for Rad26 in both TCR and transcription elongation.

PubMed: 29168508
DOI: 10.1038/nature24658

Experimental method

ELECTRON MICROSCOPY (5.8 Å)