Transcriptional activator C protein-mediated unwinding of DNA as a possible mechanism for mom gene activation
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Updated: Oct 26, 2026

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
Published on: September 20, 2018
1Microbiology and Cell Biology Department, Indian Institute of Science, Bangalore, 560 012, India.
Abstract:
The bacteriophage Mu mom gene encodes the unique DNA-modification function of the phage. Regulation of the mom gene at the transcriptional level is brought about by the transactivator protein C of the phage. The mom promoter is an activator-dependent weak promoter having poor -10 and -35 elements separated by a 19 bp suboptimal spacer region. These features could constrain RNA polymerase occupancy at the promoter. Here, we have probed into the mechanism by which C protein acts as a transcriptional activator at Pmom. In vivo dimethyl sulfate footprinting studies demonstrate C protein-mediated asymmetric distortion of its specific site at the mom regulatory region. Using a coupled topoisomerase assay, we demonstrate that C protein induces the unwinding of DNA. This C-mediated unwinding seems to be localised to the 3' flanking region of the C binding site located adjacent to and overlapping the -35 element of Pmom. These results suggest that C protein-mediated torsional changes could be reorienting the -10 and -35 elements to a favorable conformation for RNA polymerase occupancy at the mom promoter.
Insights
Bacteriophage Mu protein C activates the mom gene by distorting and unwinding DNA, improving RNA polymerase binding. This mechanism optimizes transcription of the essential mom gene for phage DNA modification.
Area of Science:
- Molecular Biology
- Genetics
- Virology
Background:
- The bacteriophage Mu mom gene is crucial for DNA modification.
- Transcriptional regulation of the mom gene is mediated by the transactivator protein C.
- The mom promoter (Pmom) is characterized by weak -10 and -35 elements and a suboptimal spacer, potentially hindering RNA polymerase binding.
Purpose of the Study:
- To elucidate the mechanism by which protein C activates transcription at the Pmom promoter.
- To investigate how protein C overcomes the suboptimal promoter structure to facilitate transcription.
Main Methods:
- In vivo dimethyl sulfate footprinting to analyze protein C interactions with the mom regulatory region.
- Coupled topoisomerase assay to assess DNA unwinding induced by protein C.
Main Results:
- Protein C binding induces asymmetric distortion of its specific site within the mom regulatory region.
- Protein C induces DNA unwinding, localized to the 3' flanking region of the C binding site, overlapping the -35 element.
- These structural changes likely reorient promoter elements for enhanced RNA polymerase occupancy.
Conclusions:
- Protein C acts as a transcriptional activator by inducing DNA torsional changes (unwinding) at the Pmom promoter.
- This mechanism facilitates RNA polymerase binding to the weak promoter elements, enabling efficient mom gene transcription.
- The findings provide insight into phage gene regulation and promoter activation strategies.
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