# Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation

## TL;DR

This paper shows how bacterial transcription and translation can be physically linked early on, allowing for regulation of gene expression through small RNA interactions.

## Contribution

The study provides structural evidence of a coupled 30S translation initiation complex and paused RNA polymerase, suggesting a new mechanism for riboregulation.

## Key findings

- The 30S translation initiation complex can associate with paused RNA polymerase near the promoter.
- mRNA in the early expressome complex can interact with small regulatory RNA and be targeted for cleavage.
- Riboregulation may enable rapid termination of gene expression in response to regulatory signals.

## Abstract

In many bacterial species, transcription and translation can be coupled physically, with potential impact on the rates and efficiency of gene expression. Here, we present structural evidence from cryo-EM demonstrating that a bacterial RNA polymerase that is paused proximally to the promoter can associate with the pioneering 30S translation initiation complex (30S IC). These findings suggest that the physical link between transcription and translation can be established prior to commitment to protein synthesis. Although the mRNA is embedded in this ‘early expressome’ complex, it can nonetheless interact with small regulatory RNA (sRNA) and be targeted for cleavage in the protein-coding region by the RNA degradosome assembly in vitro. The potential tagging of transcripts with sRNA during pioneering and subsequent stages of translation initiation, when the 30S IC is at the 5′ end of a polyribosome, may in principle contribute to efficient and rapid termination of gene expression in response to regulatory signals.

Small regulatory RNAs can act on target mRNAs to control their translation and stability. Here, the authors present evidence that this riboregulation can potentially regulate by pairing to a target site within translation initiation complex and translation-transcription assemblies.