Structural dependence of ProQ-mRNA interactions in live bacterial cells

ProQ is a post-transcriptional gene regulator in bacteria known to globally interact with both messenger RNAs (mRNAs) and small regulatory RNAs (sRNAs). Here, we investigate ProQ-mRNA interactions in live bacteria using single-molecule tracking and reveal their dependence on the structural elements of ProQ. We illustrate that during exponential growth phase, stationary phase, and osmotic stress, ProQ mainly binds to mRNAs. All structural domains of ProQ, including N-terminal domain, linker region, and C-terminal domain, contribute to mRNA binding. While residue Y70 is generally required for global mRNA binding, other tested residues in the N-terminal domain have minor to moderate effects on mRNA binding, indicating that different mRNAs likely depend on different ProQ residues for binding. Finally, our data reveal that the expressed sRNA substrates have limited impacts on the fraction of mRNA-associated ProQ, likely due to the high abundance of mRNA-free ProQ inside the cell.

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Publication Details

Journal
Communications Biology
Published
2025-12-13
DOI
https://doi.org/10.1038/s42003-025-09145-x
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
0.00

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article

Structural dependence of ProQ-mRNA interactions in live bacterial cells

Éric Massé, Marie‐Claude Carrier, Alyssa Guzman, Jingfang Mu et al.
Communications Biology
Bacterial Genetics and Biotechnology
article

Structural dependence of ProQ-mRNA interactions in live bacterial cells

Éric Massé, Marie‐Claude Carrier, Alyssa Guzman, Jingfang Mu, Karine Prévost, Jingyi Fei, Seong-Jin Park, Zunwu Zhou, Carlos Daniel Vega Valle, Nurai El Ashry
article en

Abstract

ProQ is a post-transcriptional gene regulator in bacteria known to globally interact with both messenger RNAs (mRNAs) and small regulatory RNAs (sRNAs). Here, we investigate ProQ-mRNA interactions in live bacteria using single-molecule tracking and reveal their dependence on the structural elements of ProQ. We illustrate that during exponential growth phase, stationary phase, and osmotic stress, ProQ mainly binds to mRNAs. All structural domains of ProQ, including N-terminal domain, linker region, and C-terminal domain, contribute to mRNA binding. While residue Y70 is generally required for global mRNA binding, other tested residues in the N-terminal domain have minor to moderate effects on mRNA binding, indicating that different mRNAs likely depend on different ProQ residues for binding. Finally, our data reveal that the expressed sRNA substrates have limited impacts on the fraction of mRNA-associated ProQ, likely due to the high abundance of mRNA-free ProQ inside the cell.

Communications BiologyVol. 8(1)
Université de Sherbrooke (CA), Centre Hospitalier Universitaire Sainte-Justine (CA), University of Chicago (US), Illinois Mathematics and Science Academy (US), Syracuse University (US)
National Institutes of Health, Canadian Institutes of Health Research
Openalex Percentile: Top 58%
Bacterial Genetics and Biotechnology
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