The torpedo effect in Bacillus subtilis: RNase J1 resolves stalled transcription complexes
Related Experiment Video
Updated: Jan 1, 2026

Direct Restart of a Replication Fork Stalled by a Head-On RNA Polymerase
Published on: April 29, 2010
Michaela Šiková1, Jana Wiedermannová1, Martin Převorovský2
1Institute of Microbiology of the Czech Academy of Sciences, Prague 4, Czech Republic.
Abstract:
RNase J1 is the major 5'-to-3' bacterial exoribonuclease. We demonstrate that in its absence, RNA polymerases (RNAPs) are redistributed on DNA, with increased RNAP occupancy on some genes without a parallel increase in transcriptional output. This suggests that some of these RNAPs represent stalled, non-transcribing complexes. We show that RNase J1 is able to resolve these stalled RNAP complexes by a "torpedo" mechanism, whereby RNase J1 degrades the nascent RNA and causes the transcription complex to disassemble upon collision with RNAP. A heterologous enzyme, yeast Xrn1 (5'-to-3' exonuclease), is less efficient than RNase J1 in resolving stalled Bacillus subtilis RNAP, suggesting that the effect is RNase-specific. Our results thus reveal a novel general principle, whereby an RNase can participate in genome-wide surveillance of stalled RNAP complexes, preventing potentially deleterious transcription-replication collisions.
More Related Videos
Related Concept Videos
Bacterial Transcription
Transcription can be divided into three main stages, each involving distinct DNA sequences to guide the polymerase. These are:
Coordination of Gene Expression Processes in Bacteria
Transcription Attenuation in Prokaryotes
There are several different mechanisms used to attenuate transcription. In ribosome mediated...
Bacterial RNA Polymerase
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
Bacterial RNA Polymerase
Transcription Initiation
The promoters and enhancers and their accessory proteins allow tight regulation of...

