7C17

The cryo-EM structure of E. coli CueR transcription activation complex with fully duplex promoter DNA

Summary for 7C17

• Entry DOI: 10.2210/pdb7c17/pdb
• Related: 6LDI
• EMDB information: 30268
• Descriptor: DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, SILVER ION, ... (11 entities in total)
• Functional Keywords: rna polymerase, cuer, transcription activation, transcription, transcription (dna to rna)
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 10
• Total formula weight: 539080.03

Authors

Fang, C.L.,Zhang, Y. (deposition date: 2020-05-02, release date: 2020-09-30, Last modification date: 2024-03-27)

Primary citation

Fang, C.,Philips, S.J.,Wu, X.,Chen, K.,Shi, J.,Shen, L.,Xu, J.,Feng, Y.,O'Halloran, T.V.,Zhang, Y.
CueR activates transcription through a DNA distortion mechanism.
Nat.Chem.Biol., 17:57-64, 2021

PubMed Abstract: The MerR-family transcription factors (TFs) are a large group of bacterial proteins responding to cellular metal ions and multiple antibiotics by binding within central RNA polymerase-binding regions of a promoter. While most TFs alter transcription through protein-protein interactions, MerR TFs are capable of reshaping promoter DNA. To address the question of which mechanism prevails, we determined two cryo-EM structures of transcription activation complexes (TAC) comprising Escherichia coli CueR (a prototype MerR TF), RNAP holoenzyme and promoter DNA. The structures reveal that this TF promotes productive promoter-polymerase association without canonical protein-protein contacts seen between other activator proteins and RNAP. Instead, CueR realigns the key promoter elements in the transcription activation complex by clamp-like protein-DNA interactions: these induce four distinct kinks that ultimately position the -10 element for formation of the transcription bubble. These structural and biochemical results provide strong support for the DNA distortion paradigm of allosteric transcriptional control by MerR TFs.

PubMed: 32989300
DOI: 10.1038/s41589-020-00653-x

Experimental method

ELECTRON MICROSCOPY (4.22 Å)