8X6F

Cryo-EM structure of Staphylococcus aureus sigA-dependent RNAP-promoter open complex

Summary for 8X6F

• Entry DOI: 10.2210/pdb8x6f/pdb
• EMDB information: 38087
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total)
• Functional Keywords: rna polymerase, transcription, staphylococcus aureus, siga, transcription-dna complex, transcription/dna
• Biological source: Staphylococcus aureus; More
• Total number of polymer chains: 9
• Total formula weight: 441945.86

Authors

Yuan, L.,Xu, L.,Liu, Q.,Feng, Y. (deposition date: 2023-11-21, release date: 2024-06-05, Last modification date: 2024-06-19)

Primary citation

Yuan, L.,Liu, Q.,Xu, L.,Wu, B.,Feng, Y.
Structural basis of promoter recognition by Staphylococcus aureus RNA polymerase.
Nat Commun, 15:4850-4850, 2024

PubMed Abstract: Bacterial RNAP needs to form holoenzyme with σ factors to initiate transcription. While Staphylococcus aureus σ controls housekeeping functions, S. aureus σ regulates virulence, biofilm formation, persistence, cell internalization, membrane transport, and antimicrobial resistance. Besides the sequence difference, the spacers between the -35 element and -10 element of σ regulated promoters are shorter than those of σ regulated promoters. Therefore, how σ recognizes and initiates transcription from target promoters can not be inferred from that of the well studied σ. Here, we report the cryo-EM structures of S. aureus RNAP-promoter open complexes comprising σ and σ, respectively. Structural analyses, in combination with biochemical experiments, reveal the structural basis for the promoter specificity of S. aureus transcription. Although the -10 element of σ regulated promoters is recognized by domain σ as single-stranded DNA, the -10 element of σ regulated promoters is co-recognized by domains σ and σ as double-stranded DNA, accounting for the short spacers of σ regulated promoters. S. aureus RNAP is a validated target of antibiotics, and our structures pave the way for rational drug design targeting S. aureus RNAP.

PubMed: 38844782
DOI: 10.1038/s41467-024-49229-6

Experimental method

ELECTRON MICROSCOPY (3.7 Å)