Cryo-electron microscopy (cryo-EM) is a powerful technique for determining the structures of biological macromolecular complexes. Picking single-protein particles from cryo-EM …
L You, EO Omollo, C Yu, RA Mooney, J Shi, L Shen… - Nature, 2023 - nature.com
Efficient and accurate termination is required for gene transcription in all living organisms,. Cellular RNA polymerases in both bacteria and eukaryotes can terminate their transcription …
Motivation Cryo-electron microscopy (cryo-EM) is a powerful technique for determining the structures of large protein complexes. Picking single protein particles from cryo-EM …
B Carrasco, R Torres… - FEMS microbiology …, 2024 - academic.oup.com
Accurate DNA replication and transcription elongation are crucial for preventing the accumulation of unreplicated DNA and genomic instability. Cells have evolved multiple …
Cellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening genome stability and limiting free enzyme pools, but how RNAP recycling into active states …
T Kouba, T Koval', P Sudzinová, J Pospíšil… - Nature …, 2020 - nature.com
RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we …
L Yuan, Q Liu, L Xu, B Wu, Y Feng - Nature Communications, 2024 - nature.com
Bacterial RNAP needs to form holoenzyme with σ factors to initiate transcription. While Staphylococcus aureus σA controls housekeeping functions, S. aureus σB regulates …
JJ Brewer, K Inlow, RA Mooney, B Bosch… - Nature Structural & …, 2025 - nature.com
Following transcript release during intrinsic termination, Escherichia coli RNA polymerase (RNAP) often remains associated with DNA in a post-termination complex (PTC). RNAPs in …
T Kovaľ, N Borah, P Sudzinová, B Brezovská… - Nature …, 2024 - nature.com
Mycobacterial HelD is a transcription factor that recycles stalled RNAP by dissociating it from nucleic acids and, if present, from the antibiotic rifampicin. The rescued RNAP, however …