Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Elf1 promotes Rad26's interaction with lesion-arrested Pol II for transcription-coupled repair.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 121, Issue 3, Page e2314245121, Year 2024
Publish date	Jan 16, 2024
Authors	Reta D Sarsam / Jun Xu / Indrajit Lahiri / Wenzhi Gong / Qingrong Li / Juntaek Oh / Zhen Zhou / Peini Hou / Jenny Chong / Nan Hao / Shisheng Li / Dong Wang / Andres E Leschziner /
PubMed Abstract	Transcription-coupled nucleotide excision repair (TC-NER) is a highly conserved DNA repair pathway that removes bulky lesions in the transcribed genome. Cockayne syndrome B protein (CSB), or its ...Transcription-coupled nucleotide excision repair (TC-NER) is a highly conserved DNA repair pathway that removes bulky lesions in the transcribed genome. Cockayne syndrome B protein (CSB), or its yeast ortholog Rad26, has been known for decades to play important roles in the lesion-recognition steps of TC-NER. Another conserved protein ELOF1, or its yeast ortholog Elf1, was recently identified as a core transcription-coupled repair factor. How Rad26 distinguishes between RNA polymerase II (Pol II) stalled at a DNA lesion or other obstacles and what role Elf1 plays in this process remains unknown. Here, we present cryo-EM structures of Pol II-Rad26 complexes stalled at different obstacles that show that Rad26 uses a common mechanism to recognize a stalled Pol II, with additional interactions when Pol II is arrested at a lesion. A cryo-EM structure of lesion-arrested Pol II-Rad26 bound to Elf1 revealed that Elf1 induces further interactions between Rad26 and a lesion-arrested Pol II. Biochemical and genetic data support the importance of the interplay between Elf1 and Rad26 in TC-NER initiation. Together, our results provide important mechanistic insights into how two conserved transcription-coupled repair factors, Rad26/CSB and Elf1/ELOF1, work together at the initial lesion recognition steps of transcription-coupled repair.
External links	Proc Natl Acad Sci U S A / PubMed:38194460 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 4.6 Å
Structure data	41623 8tug EMDB-41623, PDB-8tug: Cryo-EM structure of CPD-stalled Pol II in complex with Rad26 (engaged state) Method: EM (single particle) / Resolution: 3.5 Å 41647 8tvp EMDB-41647, PDB-8tvp: Cryo-EM structure of CPD-stalled Pol II in complex with Rad26 (open state) Method: EM (single particle) / Resolution: 3.7 Å 41648 8tvq EMDB-41648, PDB-8tvq: Cryo-EM structure of CPD stalled 10-subunit Pol II in complex with Rad26 Method: EM (single particle) / Resolution: 4.6 Å 41650 8tvs EMDB-41650, PDB-8tvs: Cryo-EM structure of backtracked Pol II in complex with Rad26 Method: EM (single particle) / Resolution: 4.4 Å 41652 8tvv EMDB-41652, PDB-8tvv: Cryo-EM structure of backtracked Pol II Method: EM (single particle) / Resolution: 3.7 Å 41653 8tvw EMDB-41653, PDB-8tvw: Cryo-EM structure of CPD-stalled Pol II (conformation 1) Method: EM (single particle) / Resolution: 3.6 Å 41654 8tvx EMDB-41654, PDB-8tvx: Cryo-EM structure of CPD-stalled Pol II (Conformation 2) Method: EM (single particle) / Resolution: 3.7 Å 41655 8tvy EMDB-41655, PDB-8tvy: Cryo-EM structure of CPD lesion containing RNA Polymerase II elongation complex with Rad26 and Elf1 (closed state) Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry
Source	saccharomyces cerevisiae (brewer's yeast) synthetic construct (others)
Keywords	TRANSCRIPTION/DNA/RNA / RNA Polymerase II / Rad26 / CPD lesion / Transcription-coupled DNA repair / TRANSCRIPTION / TRANSCRIPTION-DNA-RNA complex / Backtracked Polymerase