6JNX

Cryo-EM structure of a Q-engaged arrested complex

Summary for 6JNX

• Entry DOI: 10.2210/pdb6jnx/pdb
• EMDB information: 9852
• Descriptor: DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, ZINC ION, ... (11 entities in total)
• Functional Keywords: rna polymerase, antitermination, transcription, dna, rna
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 11
• Total formula weight: 542222.24

Authors

Feng, Y.,Shi, J. (deposition date: 2019-03-18, release date: 2019-06-12, Last modification date: 2024-03-27)

Primary citation

Shi, J.,Gao, X.,Tian, T.,Yu, Z.,Gao, B.,Wen, A.,You, L.,Chang, S.,Zhang, X.,Zhang, Y.,Feng, Y.
Structural basis of Q-dependent transcription antitermination.
Nat Commun, 10:2925-2925, 2019

PubMed Abstract: Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (Q and Q) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, Q forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well.

PubMed: 31266960
DOI: 10.1038/s41467-019-10958-8

Experimental method

ELECTRON MICROSCOPY (4.08 Å)