Nature Communications · 2022 · 16 citations · 35 references
Life SciencesMicrobiologyMolecular BiologyGene ExpressionTranscriptionTranscriptional RegulationRna Polymerase FunctionRna Polymerase StructureRna StructureRna TranscriptionRna-binding ProteinsTranscriptional Regulation In ProkaryotesBacterial PromotersBacterial Rna Polymerase StructureChronic Pseudomonas Aeruginosa InfectionHoloenzyme StructurePromoter Open Complex StructureRnap Holoenzyme AssemblyTranscription Initiation ComplexTranscriptional Response To Stress
Abstract Pseudomonas aeruginosa ( Pae ) SutA adapts bacteria to hypoxia and nutrition-limited environment during chronic infection by increasing transcription activity of an RNA polymerase (RNAP) holoenzyme comprising the stress-responsive σ factor σ S (RNAP-σ S ). SutA shows no homology to previously characterized RNAP-binding proteins. The structure and mode of action of SutA remain unclear. Here we determined cryo-EM structures of Pae RNAP-σ S holoenzyme, Pae RNAP-σ S holoenzyme complexed with SutA, and Pae RNAP-σ S transcription initiation complex comprising SutA. The structures show SutA pinches RNAP-β protrusion and facilitates promoter unwinding by wedging RNAP-β lobe open. Our results demonstrate that SutA clears an energetic barrier to facilitate promoter unwinding of RNAP-σ S holoenzyme.
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MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Shawn Zheng, Eugene Palovcak, Jean‐Paul Armache et al. · Nature Methods · 2017 · 8.9K citations · Full text
Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution
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