Rho-dependent transcription termination in bacteria recycles RNA polymerases stalled at DNA lesions

• Published in: Nature communications Vol. 10; no. 1; pp. 1207 - 12
• Main Authors: Jain, Sriyans, Gupta, Richa, Sen, Ranjan
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 14.03.2019; Nature Publishing Group; Nature Portfolio
• Subjects: 38; 38/23; 38/44; 42/70; 631/326/41/2532; 631/337; 631/337/1427; 82/29; Bacteria; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Cell survival; Deoxyribonucleic acid; DNA; DNA damage; DNA Damage - drug effects; DNA Damage - radiation effects; DNA helicase; DNA repair; DNA Repair - physiology; DNA, Bacterial - metabolism; DNA-Directed RNA Polymerases - metabolism; Elongation; Escherichia coli - physiology; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Humanities and Social Sciences; Lesions; Mfd protein; Mitomycin - pharmacology; multidisciplinary; Mutation; Peptide Elongation Factors - genetics; Peptide Elongation Factors - metabolism; Proteins; Repair; Ribonucleic acid; RNA; RNA helicase; RNA, Bacterial - biosynthesis; Science; Science (multidisciplinary); Transcription Factors - genetics; Transcription Factors - metabolism; Transcription termination; Transcription Termination, Genetic - physiology; Transcription-coupled repair; Ultraviolet Rays - adverse effects
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-019-09146-5

In bacteria, transcription-coupled repair of DNA lesions initiates after the Mfd protein removes RNA polymerases (RNAPs) stalled at the lesions. The bacterial RNA helicase, Rho, is a transcription termination protein that dislodges the elongation complexes. Here, we show that Rho dislodges the stalled RNAPs at DNA lesions. Strains defective in both Rho and Mfd are susceptible to DNA-damaging agents and are inefficient in repairing or propagating UV-damaged DNA. In vitro transcription assays show that Rho dissociates the stalled elongation complexes at the DNA lesions. We conclude that Rho-dependent termination recycles stalled RNAPs, which might facilitate DNA repair and other DNA-dependent processes essential for bacterial cell survival. We surmise that Rho might compete with, or augment, the Mfd function. In bacteria, the Rho protein dislodges elongation complexes to terminate transcription, and the Mfd protein removes RNA polymerases (RNAPs) stalled at DNA lesions. Here, Jain et al. show that Rho also dissociates stalled RNAPs at DNA lesions, which may facilitate DNA repair and other DNA-dependent processes.