SNAP output for PDB entry 8ftd [SNAP web server]

PDB-id

8ftd; SNAP-derived features in text and JSON formats; DNAproDB

Class

transcription, transferase-DNA

Method

cryo-EM (2.76 Å)

Summary

Structure of escherichia coli ceda in complex with transcription initiation complex

Reference

Vasilyev N, Liu MMJ, Epshtein V, Shamovsky I, Nudler E (2024): "General transcription factor from Escherichia coli with a distinct mechanism of action." Nat.Struct.Mol.Biol., 31, 141-149. doi: 10.1038/s41594-023-01154-w.

Abstract

Gene expression in Escherichia coli is controlled by well-established mechanisms that activate or repress transcription. Here, we identify CedA as an unconventional transcription factor specifically associated with the RNA polymerase (RNAP) σ₇₀ holoenzyme. Structural and biochemical analysis of CedA bound to RNAP reveal that it bridges distant domains of β and σ₇₀ subunits to stabilize an open-promoter complex. CedA does so without contacting DNA. We further show that cedA is strongly induced in response to amino acid starvation, oxidative stress and aminoglycosides. CedA provides a basal level of tolerance to these clinically relevant antibiotics, as well as to rifampicin and peroxide. Finally, we show that CedA modulates transcription of hundreds of bacterial genes, which explains its pleotropic effect on cell physiology and pathogenesis.