ArticleThe Journal of biological chemistry2016
Bacillus subtilis δ Factor Functions as a Transcriptional Regulator by Facilitating the Open Complex Formation.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 16 citations in OpenAlex.
- A noncanonical RNA polymerase assembly pathway in Bacillus subtilis: α Dimer associates with either β or β' before forming the core enzyme.The Journal of biological chemistry · 2026Article
- Transcription activation inEcoSal Plus · 2024Review
- RNA polymerases from low G+C gram-positive bacteria.Transcription · 2021Review
- Evidence of Robustness in a Two-Component System Using a Synthetic Circuit.Journal of bacteriology · 2020Article
- The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa.Molecular microbiology · 2019Article
- σJournal of bacteriology · 2018Article
- Solution structure of domain 1.1 of the σThe Journal of biological chemistry · 2017Article
- In-Culture Cross-Linking of Bacterial Cells Reveals Large-Scale Dynamic Protein-Protein Interactions at the Peptide Level.Journal of proteome research · 2017Article
- The ω Subunit Governs RNA Polymerase Stability and Transcriptional Specificity in Staphylococcus aureus.Journal of bacteriology · 2017Article
- The Blueprint of a Minimal Cell: MiniBacillus.Microbiology and molecular biology reviews : MMBR · 2016Review
- A Novel Function of δ Factor from Bacillus subtilis as a Transcriptional Repressor.The Journal of biological chemistry · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most bacterial RNA polymerases (RNAP) contain five conserved subunits, viz. 2α, β, β', and ω. However, in many Gram-positive bacteria, especially in fermicutes, RNAP is associated with an additional factor, called δ. For over three decades since its identification, it had been thought that δ functioned as a subunit of RNAP to enhance the level of transcripts by recycling RNAP. In support of the previous observations, we also find that δ is involved in recycling of RNAP by releasing the RNA from the ternary complex. We further show that δ binds to RNA and is able to recycle RNAP when the length of the nascent RNA reaches a critical length. However, in this work we decipher a new function of δ. Performing biochemical and mutational analysis, we show that Bacillus subtilis δ binds to DNA immediately upstream of the promoter element at A-rich sequences on the abrB and rrnB1 promoters and facilitates open complex formation. As a result, δ facilitates RNAP to initiate transcription in the second scale, compared with minute scale in the absence of δ. Using transcription assay, we show that δ-mediated recycling of RNAP cannot be the sole reason for the enhancement of transcript yield. Our observation that δ does not bind to RNAP holo enzyme but is required to bind to DNA upstream of the -35 promoter element for transcription activation suggests that δ functions as a transcriptional regulator.
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