Transcription termination factor rho is an RNA-DNA helicase - PubMed (original) (raw)
Transcription termination factor rho is an RNA-DNA helicase
C A Brennan et al. Cell. 1987.
Abstract
E. coli rho factor can unwind a short RNA-DNA duplex in vitro. The duplex is formed between a polylinker sequence at the 3' end of RNA derived from the rho-dependent terminator trp t' and the complementary sequence in a single-strand DNA molecule. Release of trp t' RNA from the duplex requires nucleoside triphosphate hydrolysis by rho's NTPase activity and is dependent on rho recognition of the RNA that is 5' to the RNA-DNA duplex region. The direction of helix unwinding appears to be 5' to 3' along the RNA molecule. These characteristics now account for how the RNA-binding and RNA-dependent NTP hydrolysis activities of rho may participate directly in transcription termination. Our results suggest that NTP hydrolysis is utilized to help unwind the RNA-DNA duplex at the 3' end of a nascent transcript, facilitating RNA release from the DNA template.
Similar articles
- Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 2. Processivity, ATP consumption, and RNA binding.
Walstrom KM, Dozono JM, von Hippel PH. Walstrom KM, et al. Biochemistry. 1997 Jul 1;36(26):7993-8004. doi: 10.1021/bi963180r. Biochemistry. 1997. PMID: 9201946 - Rho-dependent termination and concomitant NTPase activity requires a specific, intact RNA region.
Sharp JA, Platt T. Sharp JA, et al. J Biol Chem. 1984 Feb 25;259(4):2268-73. J Biol Chem. 1984. PMID: 6199348 - Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 1. Characterization and analysis of the reaction.
Walstrom KM, Dozono JM, Robic S, von Hippel PH. Walstrom KM, et al. Biochemistry. 1997 Jul 1;36(26):7980-92. doi: 10.1021/bi963179s. Biochemistry. 1997. PMID: 9201945 - Rho-dependent transcription termination: more questions than answers.
Banerjee S, Chalissery J, Bandey I, Sen R. Banerjee S, et al. J Microbiol. 2006 Feb;44(1):11-22. J Microbiol. 2006. PMID: 16554712 Free PMC article. Review. - Rho and RNA: models for recognition and response.
Platt T. Platt T. Mol Microbiol. 1994 Mar;11(6):983-90. doi: 10.1111/j.1365-2958.1994.tb00376.x. Mol Microbiol. 1994. PMID: 8022288 Review.
Cited by
- A widely conserved protein Rof inhibits transcription termination factor Rho and promotes Salmonella virulence program.
Zhang J, Zhang S, Zhou W, Zhang X, Li G, Li R, Lin X, Chen Z, Liu F, Shen P, Zhou X, Gao Y, Chen Z, Chao Y, Wang C. Zhang J, et al. Nat Commun. 2024 Apr 15;15(1):3187. doi: 10.1038/s41467-024-47438-7. Nat Commun. 2024. PMID: 38622116 Free PMC article. - A trailing ribosome speeds up RNA polymerase at the expense of transcript fidelity via force and allostery.
Wee LM, Tong AB, Florez Ariza AJ, Cañari-Chumpitaz C, Grob P, Nogales E, Bustamante CJ. Wee LM, et al. Cell. 2023 Mar 16;186(6):1244-1262.e34. doi: 10.1016/j.cell.2023.02.008. Cell. 2023. PMID: 36931247 Free PMC article. - Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase from Thermus thermophilus.
Murayama Y, Ehara H, Aoki M, Goto M, Yokoyama T, Sekine SI. Murayama Y, et al. Sci Adv. 2023 Feb 10;9(6):eade7093. doi: 10.1126/sciadv.ade7093. Epub 2023 Feb 8. Sci Adv. 2023. PMID: 36753546 Free PMC article. - Structural basis of Rho-dependent transcription termination.
Molodtsov V, Wang C, Firlar E, Kaelber JT, Ebright RH. Molodtsov V, et al. Nature. 2023 Feb;614(7947):367-374. doi: 10.1038/s41586-022-05658-1. Epub 2023 Jan 25. Nature. 2023. PMID: 36697824 Free PMC article. - Protein structure terminates doubt about how transcription stops.
Rashid F, Berger J. Rashid F, et al. Nature. 2023 Feb;614(7947):237-238. doi: 10.1038/d41586-023-00121-1. Nature. 2023. PMID: 36697726 No abstract available.
Publication types
MeSH terms
Substances
LinkOut - more resources
Molecular Biology Databases