ArticleNucleic acids research2012
RNA polymerase-promoter interactions determining different stability of the Escherichia coli and Thermus aquaticus transcription initiation complexes.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- The -10 region adjacent to open reading frames is a common expression pattern inLife science alliance · 2025Article
- The effect of pseudoknot base pairing on cotranscriptional structural switching of the fluoride riboswitch.Nucleic acids research · 2024Article
- CarD contributes to diverse gene expression outcomes throughout the genome ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Backtracked and paused transcription initiation intermediate of Escherichia coli RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- RNA polymerase molecular beacon as tool for studies of RNA polymerase-promoter interactions.Methods (San Diego, Calif.) · 2015Review
- Mycobacterial RNA polymerase forms unstable open promoter complexes that are stabilized by CarD.Nucleic acids research · 2015Article
- Coupling of downstream RNA polymerase-promoter interactions with formation of catalytically competent transcription initiation complex.Journal of molecular biology · 2014Article
- Cooperativity and interaction energy threshold effects in recognition of the -10 promoter element by bacterial RNA polymerase.Nucleic acids research · 2013Article
- Biochemical insights into the function of phage G1 gp67 in Staphylococcus aureus.Bacteriophage · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Transcription initiation complexes formed by bacterial RNA polymerases (RNAPs) exhibit dramatic species-specific differences in stability, leading to different strategies of transcription regulation. The molecular basis for this diversity is unclear. Promoter complexes formed by RNAP from Thermus aquaticus (Taq) are considerably less stable than Escherichia coli RNAP promoter complexes, particularly at temperatures below 37°C. Here, we used a fluorometric RNAP molecular beacon assay to discern partial RNAP-promoter interactions. We quantitatively compared the strength of E. coli and Taq RNAPs partial interactions with the -10, -35 and UP promoter elements; the TG motif of the extended -10 element; the discriminator and the downstream duplex promoter segments. We found that compared with Taq RNAP, E. coli RNAP has much higher affinity only to the UP element and the downstream promoter duplex. This result indicates that the difference in stability between E. coli and Taq promoter complexes is mainly determined by the differential strength of core RNAP-DNA contacts. We suggest that the relative weakness of Taq RNAP interactions with DNA downstream of the transcription start point is the major reason of low stability and temperature sensitivity of promoter complexes formed by this enzyme.
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