ArticleNucleic acids research2026
Structural basis for loading of transcription repair-coupling factor Mfd onto stalled elongation complexes.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Transcription-coupled repair (TCR) is a nucleotide excision repair sub-pathway that preferentially removes lesions from the DNA template-strand that stall RNA polymerase elongation complexes (ECs). In bacteria, the superfamily 2 Mfd translocase mediates TCR by displacing stalled ECs and recruiting Uvr(A)B. Using cryo-electron microscopy, we previously visualized seven Mfd-EC complexes spanning the ATP-dependent Mfd loading and EC displacement pathway [L1 → L2(ADP) → C1(ATP) → C2(ATP) → C3(ADP) → C4(ADP) → C5(ATP)]. The first intermediate (L1) was poorly resolved (4.1 Å nominal resolution) due to low particle occupancy. The pathway is characterized by very large Mfd structural transitions, notably the L1 → L2 transition. Here, we pre-loaded Mfd with ATP in the presence of the γ-phosphate mimic, BeF3-, limiting rounds of ATP hydrolysis. The resulting accumulation of early intermediates allowed us to resolve the L1 intermediate to 3.5 Å nominal resolution, revealing bound ADP-BeF3-. We also identified a new intermediate between L1 and L2, L1.5, providing further insight into Mfd conformational changes during loading.
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